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Journal articles on the topic 'S-ribonuclease'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Diaz-Baena, Mercedes, Elena Delgado-García, Manuel Pineda, Gregorio Galvez-Valdivieso, and Pedro Piedras. "S-Like Ribonuclease T2 Genes Are Induced during Mobilisation of Nutrients in Cotyledons from Common Bean." Agronomy 11, no. 3 (March 6, 2021): 490. http://dx.doi.org/10.3390/agronomy11030490.

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Germination and seedling development are crucial phases in a plant’s life cycle with economical and agronomical implications. The RNA quality in seeds is linked to seed viability, being an important agronomic trait since this leads to a loss in germination efficiency. In addition, RNA can be an important phosphorous reservoir in seeds, affecting the efficiency of the mobilisation of nutrients towards the seedlings. However, knowledge about the physiological function of ribonucleases during germination and seedling development is scarce. We analysed the ribonuclease activities of cotyledons during these processes and the expression of S-like ribonucleases T2. Ribonuclease activity was detected in cotyledons at 1 day after imbibition and the specific activity increased during germination and seedling development, reaching a maximal value at 10 days after imbibition. At this stage, the levels of proteins and RNA in cotyledons were very low. Using in-gel assays, three ribonucleases were detected with apparent molecular masses of 16, 17 and 19 kDa along cotyledon ontogeny. The S-like ribonucleases T2 family consists of four genes in common bean (PvRNS1 to PvRNS4). The expression of PvRNS1, PvRNS2 and PvRNS4 increased in the phase of nutrient mobilisation in cotyledons. The expression of PvRNS1 increased 1000 fold in cotyledons, from 1 to 6 days after imbibition. The suppression of the induction of ribonuclease activity and gene expression in decapitated seedlings suggests that the regulatory signal comes from the developing axes. These results clearly state that S-like ribonucleases T2 are involved in RNA turnover in cotyledons during seedling development.

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2

Watkins, Rex W., Ulrich Arnold, and Ronald T. Raines. "Ribonuclease S redux." Chem. Commun. 47, no. 3 (2011): 973–75. http://dx.doi.org/10.1039/c0cc03864d.

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3

Nadig, Gautham, Girish S. Ratnaparkhi, Raghavan Varadarajan, and Saraswathi Vishveshwara. "Dynamics of ribonuclease A and ribonuclease S: Computational and experimental studies." Protein Science 5, no. 10 (October 1996): 2104–14. http://dx.doi.org/10.1002/pro.5560051017.

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4

Zuckermann, Ronald N., and Peter G. Schultz. "A hybrid sequence-selective ribonuclease S." Journal of the American Chemical Society 110, no. 19 (September 1988): 6592–94. http://dx.doi.org/10.1021/ja00227a066.

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5

Asano, Koji, Shozo Fujita, Toshiya Senda, and Yukio Mitsui. "Crystal growth of ribonuclease S under microgravity." Journal of Crystal Growth 122, no. 1-4 (August 1992): 323–29. http://dx.doi.org/10.1016/0022-0248(92)90264-j.

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6

Ehrat, Markus, Douglas J. Cecchini, and Roger W. Giese. "Substrate-Leash Amplification with Ribonuclease S-Peptide and S-Protein." Clinical Chemistry 32, no. 2 (February 1, 1986): 390. http://dx.doi.org/10.1093/clinchem/32.2.390.

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Abstract p 1628, Fig. 6: Although faint, there is a band at the origin in lane g. p 1656: The accompanying figure should be substituted for the Figure 2 shown on page 1656, a figure that was to have been deleted. The figure legend is unchanged. p 1705: The second paragraph in the left column should replace the third paragraph of the Discussion. Thus the authors find it "likely...that the principal alkali-labile oxalate precursors in urine are ascorbate and some of its metabolites...." p 1927: The name of the author of a book review, Robert Rej, was omitted. p 2014: On line 7, the 95 percentile interval for plasma ammonia should be 16-53 µmol/L, as correctly stated in the Abstract. See image in the PDF file

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7

Ehrat, M., D. J. Cecchini, and R. W. Giese. "Substrate-leash amplification with ribonuclease S-peptide and S-protein." Clinical Chemistry 32, no. 9 (September 1, 1986): 1622–30. http://dx.doi.org/10.1093/clinchem/32.9.1622.

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Abstract The S-peptide and S-protein fragments of ribonuclease S (RNase S, no EC no. assigned) have been immobilized onto separate Sepharose gels via a "leash" of polycytidylic acid substrate. Each of these gels releases its RNase fragment when treated with the complementary enzyme fragment or with RNase A (EC 3.1.27.5), and the released fragments recombine to give RNase S activity. Thus this system provides substrate-leash amplification (SLA), such that more enzymatic activity is eluted from the system than is applied. For example, 100 pg of RNase applied to the S-peptide gel is amplified by 1.9 X 10(4) to the equivalent of 1.9 micrograms of activity in 20 h, when followed by combination of the released S-peptide with excess S-protein. We also tested a three-stage amplification system, with a pair of S-peptide and S-protein gels at each stage. In this system the cumulative amplification of the initial 1-ng dose of RNase A is 4.9, 52, and 25-fold after each stage, respectively. Only 2 mg of each SLA gel is used per stage in these experiments, reflecting the magnitude of their production of RNase S activity.

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8

Hamachi, Itaru, Yasuhiro Yamada, Ryoji Eboshi, Takashi Hiraoka, and Seiji Shinkai. "Design and semisynthesis of spermine-sensitive ribonuclease S'." Bioorganic & Medicinal Chemistry Letters 9, no. 9 (May 1999): 1215–18. http://dx.doi.org/10.1016/s0960-894x(99)00189-4.

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9

Nishimura, Emi, Minako Kawahara, Reina Kodaira, Marina Kume, Naoki Arai, Jun-ichi Nishikawa, and Takashi Ohyama. "S-like ribonuclease gene expression in carnivorous plants." Planta 238, no. 5 (August 20, 2013): 955–67. http://dx.doi.org/10.1007/s00425-013-1945-6.

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10

Scolaro, Barbara, Laura Biondi, Fernando Filira, and Raniero Rocchi. "Semisynthetic glycoproteins: preparation of glycosylated ribonuclease S′ analogues." Reactive Polymers 22, no. 3 (June 1994): 195–201. http://dx.doi.org/10.1016/0923-1137(94)90117-1.

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11

Haris, Parvez I., David C. Lee, and Dennis Chapman. "A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 874, no. 3 (December 1986): 255–65. http://dx.doi.org/10.1016/0167-4838(86)90024-5.

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12

Takeda, Naohiro, Minoru Kato, and Yoshihiro Taniguchi. "Pressure-induced secondary structure changes of ribonuclease A and ribonuclease S studied by FTIR spectroscopy." Biospectroscopy 1, no. 3 (1995): 207–16. http://dx.doi.org/10.1002/bspy.350010305.

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13

Pal-Bhowmick, Ipsita, Ramendra Pati Pandey, Gotam K. Jarori, Santosh Kar, and Dinkar Sahal. "Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides." Biochemical and Biophysical Research Communications 364, no. 3 (December 2007): 608–13. http://dx.doi.org/10.1016/j.bbrc.2007.10.056.

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14

McElligott, M. A., P. Miao, and J. F. Dice. "Lysosomal degradation of ribonuclease A and ribonuclease S-protein microinjected into the cytosol of human fibroblasts." Journal of Biological Chemistry 260, no. 22 (October 1985): 11986–93. http://dx.doi.org/10.1016/s0021-9258(17)38974-3.

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15

Travis Gallagher, D., Carrie Stover, David Charlton, Leonard Arnowitz, and David R. Black. "X-ray topography of microgravity-grown ribonuclease S crystals." Journal of Crystal Growth 255, no. 3-4 (August 2003): 403–13. http://dx.doi.org/10.1016/s0022-0248(03)01309-5.

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16

Catanzano, Francesca, Concetta Giancola, Giuseppe Graziano, and Guido Barone. "Temperature-Induced Denaturation of Ribonuclease S: A Thermodynamic Study†." Biochemistry 35, no. 41 (January 1996): 13378–85. http://dx.doi.org/10.1021/bi960855h.

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17

Kim, Jin-Soo, and Ronald T. Raines. "Ribonuclease S-peptide as a carrier in fusion proteins." Protein Science 2, no. 3 (December 31, 2008): 348–56. http://dx.doi.org/10.1002/pro.5560020307.

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18

Pulido, Daniel, Jorge Pedro López-Alonso, Vicente Marchán, Carlos González, Anna Grandas, and Douglas V. Laurents. "Preparation of Ribonuclease S Domain-Swapped Dimers Conjugated with DNA and PNA: Modulating the Activity of Ribonucleases." Bioconjugate Chemistry 19, no. 1 (January 2008): 263–70. http://dx.doi.org/10.1021/bc700374q.

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19

Kim, Eunice E., Raghavan Varadarajan, Harold W. Wyckoff, and Frederic M. Richards. "Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures." Biochemistry 31, no. 49 (December 15, 1992): 12304–14. http://dx.doi.org/10.1021/bi00164a004.

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20

Stelea, Simona D., and Timothy A. Keiderling. "Pretransitional Structural Changes in the Thermal Denaturation of Ribonuclease S and S Protein." Biophysical Journal 83, no. 4 (October 2002): 2259–69. http://dx.doi.org/10.1016/s0006-3495(02)73986-6.

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21

Hegedüs, Attila, Zoltán Szabó, József Nyéki, Júlia Halász, and Andrzej Pedryc. "Molecular Analysis of S-haplotypes in Peach, a Self-compatible Prunus Species." Journal of the American Society for Horticultural Science 131, no. 6 (November 2006): 738–43. http://dx.doi.org/10.21273/jashs.131.6.738.

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The most commercially grown peach [Prunus persica (L.) Batsch.] cultivars do not require cross-pollination for reasonable fruit set; however, self-incompatibility is a well-known feature within the Prunoideae subfamily. Isoelectric focusing and native polyacrylamide gel electrophoresis of S-ribonucleases; PCR analyses of S-RNase and S-haplotype-specific F-box genes as well as DNA sequencing were carried out to survey the self-(in)compatibility allele pool and to uncover the nature of self-compatibility in peach. From 25 cultivars and hybrids with considerable diversity in phenotype and origin, only two S-haplotypes were detected. Allele identity could be checked by exact length determination of the PCR-amplified fragments and/or partial sequencing of the peach S1-, S2-, and Prunus davidiana (Carr.) Franch. S1-RNases. S-RNases of peach were detected to possess ribonuclease activity, and a single nucleotide polymorphism in the S1-RNase was shown, which represents a synonymous substitution and does not change the amino acid present at the position in the protein. A 700-bp fragment of the peach SFB gene was PCR-amplified, which is similar to the fragment size of functional Prunus L. SFBs. All data obtained in this study may support the contribution of genes outside the S-locus to the self-compatible phenotype of peaches.

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22

Weizhong, Ke, and Wu Jianzhong. "Influence of the Nitrobenzene Extraction Technique on the Protein Molecule Conformation." Applied Spectroscopy 48, no. 2 (February 1994): 209–13. http://dx.doi.org/10.1366/0003702944028506.

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The Raman spectra of lysozyme, ribonuclease, and BSA (bovine serum albumin) in aqueous solution extracted by nitrobenzene and the ultraviolet visible absorption spectra of BSA in aqueous solution have been studied. It has been proven that the structure of all the characteristic Raman and UV bands of BAS protein in aqueous solution is due to α;-helical and random-coil conformations. The tyrosine residue is “exposed”, and the conformation of the carbon atoms in the disulfide bridge c-c-s-s-c-c is trans-gauche-gauche. The influence of adding nitrobenzene to lysozyme, ribonuclease, and BSA aqueous solution has been studied. The study indicated that nitrobenzene treatment of protein aqueous solution is an efficient means for obtaining better Raman spectra.

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23

Vetter, W. M., D. T. Gallagher, and M. Dudley. "Synchrotron white-beam X-ray topography of ribonuclease S crystals." Acta Crystallographica Section D Biological Crystallography 58, no. 4 (March 22, 2002): 579–84. http://dx.doi.org/10.1107/s090744490200121x.

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24

James, D. Andrew, Darcy C. Burns, and G. Andrew Woolley. "Kinetic characterization of ribonuclease S mutants containing photoisomerizable phenylazophenylalanine residues." Protein Engineering, Design and Selection 14, no. 12 (December 2001): 983–91. http://dx.doi.org/10.1093/protein/14.12.983.

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25

Liu, David, John Karanicolas, Catherine Yu, Zhihua Zhang, and G. Andrew Woolley. "Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S." Bioorganic & Medicinal Chemistry Letters 7, no. 20 (October 1997): 2677–80. http://dx.doi.org/10.1016/s0960-894x(97)10044-0.

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26

Fafarman, Aaron T., and Steven G. Boxer. "Nitrile Bonds as Infrared Probes of Electrostatics in Ribonuclease S." Journal of Physical Chemistry B 114, no. 42 (October 28, 2010): 13536–44. http://dx.doi.org/10.1021/jp106406p.

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27

Genz, Maika, Valentin Köhler, Michel Krauss, David Singer, Ralf Hoffmann, Thomas R. Ward, and Norbert Sträter. "An Artificial Imine Reductase based on the Ribonuclease S Scaffold." ChemCatChem 6, no. 3 (February 3, 2014): 736–40. http://dx.doi.org/10.1002/cctc.201300995.

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28

Ratnaparkhi, Girish S., and R. Varadarajan. "X-ray crystallographic studies of the denaturation of ribonuclease S." Proteins: Structure, Function, and Genetics 36, no. 3 (August 15, 1999): 282–94. http://dx.doi.org/10.1002/(sici)1097-0134(19990815)36:3<282::aid-prot3>3.0.co;2-f.

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29

Nelson, Jeffrey W., and Neville R. Kallenbach. "Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol." Proteins: Structure, Function, and Genetics 1, no. 3 (March 1986): 211–17. http://dx.doi.org/10.1002/prot.340010303.

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30

Schleker, Wolfgang, and Jörg Fleischhauer. "Zum Circulardichroismus von Disulfidbrücken in Proteinen. Teil 2. Vergleichende CNDO/S- und INDO/S-CI-Rechnungen." Zeitschrift für Naturforschung A 42, no. 4 (April 1, 1987): 361–66. http://dx.doi.org/10.1515/zna-1987-0404.

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Rotatory strengths for H2S2 conformers based on X-ray data for ribonuclease A, 2-, and 4-zinc-insuline-dimers have been calculated with some CNDO/S- and INDO/S-versions. The best agreement between their calculated signs and those predicted by the quadrant rule and Rauk’s valence basis set ab initio calculations are found with the CNDUV-version of CNDO/S. A choice of β0s = - 11.5 eV within this method improves the calculated transition wavelengths compared to observed ones.

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31

Marchiori, Fernando, Gianfranco Borin, and Luis Moroder. "STUDIES ON RIBONUCLEASE S: THE ROLE OF LYSINE-7 FOR ACTIVATION OF S-PROTEIN*." International Journal of Peptide and Protein Research 6, no. 6 (January 12, 2009): 419–34. http://dx.doi.org/10.1111/j.1399-3011.1974.tb02403.x.

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32

Hegedűs, Attila, Júlia Halász, Zoltán Szabó, József Nyéki, and Andrzej Pedryc. "How does the S-locus determining self-incompatibility in stone fruits work in self-compatible peach?" Acta Agraria Debreceniensis, no. 17 (September 14, 2005): 93–100. http://dx.doi.org/10.34101/actaagrar/17/3277.

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The majority of stone fruit species are self-incompatible, a feature that is determined by a specific recognition mechanism between the S-ribonuclease enzymes residing in the pistils and the F-box proteins expressed in the pollen tubes. Failure in the function of any component of this bipartite system resulted in self-compatibility (SC) in many cultivars of Prunus species. Peach (Prunus persica (L.) Batsch.) is the only species in the Prunoideae subfamily that is traditionally known to be self-compatible, but its molecular background is completely unknown. Isoelectric focusing and S-gene specific PCR revealed that SC is not due to functional inability of pistil ribonucleases. We hypothesize that SC may be a consequence of a kind of pollen-part mutation or the action of one or more currently unknown modifier gene(s). Only two S-alleles were identified in a set of peach genotypes of various origin and phenotypes in contrast to the 17–30 alleles described in self-incompatible fruit trees. Most important commercial cultivars carry the same S-allele and are in a homozygote state. This indicates the common origin of these cultivars and also the consequence of self-fertilization. According to the available information, this is the first report to elucidate the role of S-locus in the fertilization process of peach.

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33

Jankovic, Dragana, Svenja Steinfelder, John F. Andersen, and Alan Sher. "Helminth secretory product Ribonuclease T2 is a Th2-inducing agent (43.8)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S37. http://dx.doi.org/10.4049/jimmunol.178.supp.43.8.

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Abstract Helminth-induced Th2 polarization is associated with down-regulated dendritic cell (DC) function but the underlying molecular mechanism remains elusive due to the poor characterization of helminth molecules with Th2-inducing activity. During Schistosoma mansoni infection egg, but not worm, Ag are a target of a strong Th2 response. Moreover, when injected in naïve mice schistosome eggs or water-soluble egg extract (SEA) have an intrinsic ability to promote development of Th2 cells. Using as a read-out an in vitro model of CD4+ T cell priming with CD11c+ splenic DC we demonstrated that SEA fractions containing molecule(s) with an approximate MW of 30 kD selectively promote Th2 polarization and down-regulate DC functions. Moreover, similar positive fractions were isolated from preparations containing egg excretory/secretory molecules. The N-terminal sequence of the latter identified the S. mansoni enzyme Ribonuclease T2 as the active component and this was further confirmed with the recombinant protein. S. mansoni ribonuclease is the first chemically defined protein with Th2-promoting activity known to act on dendritic cells.

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34

Gilmanshin, Rudolf, Jeroen Van Beek, and Robert Callender. "Study of the Ribonuclease S-Peptide/S-Protein Complex by Means of Raman Difference Spectroscopy." Journal of Physical Chemistry 100, no. 41 (January 1996): 16754–60. http://dx.doi.org/10.1021/jp9611941.

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35

Loo, Rachel R. Ogorzalek, David R. Goodlett, Richard D. Smith, and Joseph A. Loo. "Observation of a noncovalent ribonuclease S-protein/S-peptide complex by electrospray ionization mass spectrometry." Journal of the American Chemical Society 115, no. 10 (May 1993): 4391–92. http://dx.doi.org/10.1021/ja00063a079.

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36

CORIGLIANO-MURPHY, M. ANGELA, XUN LIANG, CYRIL PONNAMPERUMA, DANIELE DALZOPPO, ANGELO FONTANA, TATSUHIKO KANMERA, and IRWIN M. CHAIKEN. "Synthesis and properties of an all-D model ribonuclease S-peptide." International Journal of Peptide and Protein Research 25, no. 3 (January 12, 2009): 225–31. http://dx.doi.org/10.1111/j.1399-3011.1985.tb02168.x.

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37

Tanaka, T., and Y. Kikuchi. "Mutational analysis on the S-domain of bacterial ribonuclease P ribozyme." Nucleic Acids Symposium Series 51, no. 1 (November 1, 2007): 371–72. http://dx.doi.org/10.1093/nass/nrm186.

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38

Smith, George P., David A. Schultz, and John E. Ladbury. "A ribonuclease S-peptide antagonist discovered with a bacteriophage display library." Gene 128, no. 1 (June 1993): 37–42. http://dx.doi.org/10.1016/0378-1119(93)90150-2.

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39

Ratnaparkhi, Girish S., and Raghavan Varadarajan. "Osmolytes Stabilize Ribonuclease S by Stabilizing Its Fragments S Protein and S Peptide to Compact Folding-competent States." Journal of Biological Chemistry 276, no. 31 (May 23, 2001): 28789–98. http://dx.doi.org/10.1074/jbc.m101906200.

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40

Ratnaparkhi, Girish S., Satish Kumar Awasthi, P. Rani, P. Balaram, and R. Varadarajan. "Structural and thermodynamic consequences of introducing α-aminoisobutyric acid in the S peptide of ribonuclease S." Protein Engineering, Design and Selection 13, no. 10 (October 2000): 697–702. http://dx.doi.org/10.1093/protein/13.10.697.

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41

Pechik, I. V., and G. L. Gilliland. "Crystallization and refined structure of ribonuclease S complexed with a substrate analog." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C165. http://dx.doi.org/10.1107/s0108767396092665.

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42

Chun, P. W. "A Thermodynamic Molecular Switch in Biological Systems: Ribonuclease S' Fragment Complementation Reactions." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A410. http://dx.doi.org/10.1042/bst028a410b.

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43

Varadarajan, Raghavan, Patrick R. Connelly, Julian M. Sturtevant, and Frederic M. Richards. "Heat capacity changes for protein-peptide interactions in the ribonuclease S system." Biochemistry 31, no. 5 (February 11, 1992): 1421–26. http://dx.doi.org/10.1021/bi00120a019.

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44

Chun, Paul W. "A Thermodynamic Molecular Switch in Biological Systems: Ribonuclease S′ Fragment Complementation Reactions." Biophysical Journal 78, no. 1 (January 2000): 416–29. http://dx.doi.org/10.1016/s0006-3495(00)76604-5.

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45

Kresge, Nicole, Robert D. Simoni, and Robert L. Hill. "Structure-Function Relationships in Ribonuclease S: the Work of Frederic M. Richards." Journal of Biological Chemistry 284, no. 39 (September 2009): e14-e15. http://dx.doi.org/10.1016/s0021-9258(20)38533-1.

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46

Backer, Marina V., Timur I. Gaynutdinov, Renee Aloise, Kristen Przekop, and Joseph M. Backer. "Engineering S-protein fragments of bovine ribonuclease A for targeted drug delivery." Protein Expression and Purification 26, no. 3 (December 2002): 455–61. http://dx.doi.org/10.1016/s1046-5928(02)00546-6.

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47

Mcclure, BA, V. Haring, PR Ebert, MA Anderson, A. Bacic, and AE Clarke. "Molecular Genetics and Biology of Self-Incompatibility in Nicotiana alata, an Ornamental Tobacco." Functional Plant Biology 17, no. 3 (1990): 345. http://dx.doi.org/10.1071/pp9900345.

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Glycoproteins are present in the styles of several self-incompatible species within the Solanaceae which segregate with particular alleles of the S-(self-incompatibility) gene. The amino acid sequences of style glycoproteins corresponding to different S-alleles of N. alata are homologous in some regions and variable in others. Homologous regions include N-terminal sequences as well as most of the glycosylation sites and cysteine residues. The isolated style S-glycoproteins inhibit in vitro growth of pollen tubes of several S-genotypes, with some specificity in the interaction. The isolated S-glycoproteins have ribonuclease activity which may be involved in their action in arrest of growth of incompatible (self) pollen.

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48

Abruscato, Vincenzo, Graziella Ranghino, and Anna Maria Villa. "Conformational Behaviour of an Analogue of the S-Peptide: A Molecular Dynamics Study." Protein & Peptide Letters 3, no. 4 (August 1996): 275–82. http://dx.doi.org/10.2174/092986650304220615162309.

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Abstract: The S-peptide, derived from the hydrolysis of Ribonuclease, is a stable a.-helix in water, although it is only 20 amino acids long. In view of increasing the helical content and stability, a mutated sequence has been proposed. The present work aims to shed light on the conformational preferences and on the helix stability of the proposed sequence by means of Molecular Dynamics simulations performed with different procedures.

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49

Ha, Lisha, Jennifer Colquhoun, Nicholas Noinaj, Chittaranjan Das, Paul M. Dunman, and Daniel P. Flaherty. "Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus." Acta Crystallographica Section F Structural Biology Communications 74, no. 10 (September 19, 2018): 632–37. http://dx.doi.org/10.1107/s2053230x18011512.

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Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 Å resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5′-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections.

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50

Chun, Paul W. "Planck−Benzinger Thermal Work Function: Thermodynamic Approach to Site-Specific S-Protein and S-Peptides Interactions in the Ribonuclease S‘ System." Journal of Physical Chemistry B 101, no. 39 (September 1997): 7835–43. http://dx.doi.org/10.1021/jp9703364.

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