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Relevant bibliographies by topics / Octapeptide repeat region

Academic literature on the topic 'Octapeptide repeat region'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Octapeptide repeat region"

1

Görnhardt, Birgit, Ila Rouhara, and Elmon Schmelzer. "Cyst Germination Proteins of the Potato Pathogen Phytophthora infestans Share Homology with Human Mucins." Molecular Plant-Microbe Interactions® 13, no. 1 (January 2000): 32–42. http://dx.doi.org/10.1094/mpmi.2000.13.1.32.

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We have cloned genes of Phytophthora infestans, the causal agent of potato late blight, that are activated shortly before the onset of invasion of the host tissue. The three genes isolated appear to be arranged in a genomic cluster and belong to a small polymorphic gene family. A conspicuous feature of the deduced proteins is an internal octapeptide repeat with the consensus sequence TTYAP TEE. Because of this structural motif, these novel P. infestans proteins were named Car (cyst-germination-specific acidic repeat) proteins. One of the genes, car90, codes for 1,489 amino acids including 120 octapeptide tandem repeats. Car proteins are transiently expressed during germination of cysts and formation of appressoria and are localized at the surface of germlings. The structural motif of tandemly repeated oligopeptides also occurs in a prominent class of proteins, the mucins, from mammals. The P. infestans Car proteins share 51% sequence homology with the tandem repeat region of a subfamily of human mucins. According to the physiological functions ascribed to mucins, we suggest that Car proteins may serve as a mucous cover protecting the germling from desiccation, physical damage, and adverse effects of the plant defense response and may assist in adhesion to the leaf surface.

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2

Hara, Hideyuki, and Suehiro Sakaguchi. "N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases." International Journal of Molecular Sciences 21, no. 17 (August 28, 2020): 6233. http://dx.doi.org/10.3390/ijms21176233.

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The normal cellular isoform of prion protein, designated PrPC, is constitutively converted to the abnormally folded, amyloidogenic isoform, PrPSc, in prion diseases, which include Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals. PrPC is a membrane glycoprotein consisting of the non-structural N-terminal domain and the globular C-terminal domain. During conversion of PrPC to PrPSc, its 2/3 C-terminal region undergoes marked structural changes, forming a protease-resistant structure. In contrast, the N-terminal region remains protease-sensitive in PrPSc. Reverse genetic studies using reconstituted PrPC-knockout mice with various mutant PrP molecules have revealed that the N-terminal domain has an important role in the normal function of PrPC and the conversion of PrPC to PrPSc. The N-terminal domain includes various characteristic regions, such as the positively charged residue-rich polybasic region, the octapeptide repeat (OR) region consisting of five repeats of an octapeptide sequence, and the post-OR region with another positively charged residue-rich polybasic region followed by a stretch of hydrophobic residues. We discuss the normal functions of PrPC, the conversion of PrPC to PrPSc, and the neurotoxicity of PrPSc by focusing on the roles of the N-terminal regions in these topics.

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3

Hreško, Stanislav, and Ľudmila Tkáčiková. "Variation in the coding region of the prion protein gene in Slovak cattle." Acta Veterinaria Hungarica 60, no. 2 (June 1, 2012): 233–43. http://dx.doi.org/10.1556/avet.2012.020.

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This study was conducted to investigate the presence of single nucleotide polymorphisms (SNPs) in the coding region of the bovine prion protein (PrP) gene among healthy and bovine spongiform encephalopathy (BSE-) affected cattle in Slovakia. Denaturing gradient gel electrophoresis (DGGE) and single-strand conformation polymorphism (SSCP) followed by DNA sequencing were used to identify SNPs and variations in octapeptide repeats. Altogether three single nucleotide polymorphisms (g234a, c339t and c576t) and variations in the number of octapeptide repeat units (5 or 6) were found in the analysed part of the prion protein gene. All single nucleotide polymorphisms were silent, causing no amino acid changes. Significant differences (P < 0.05) in the genotype distribution of g234a polymorphism were observed when the homozygous genotype with a mutated allele (caa/caa) was compared to the heterozygous genotype -/cag among healthy and BSE-affected cattle. The homozygous genotype caa/caa was characteristic of the group of BSE-affected cattle. Additionally, the homozygous genotype caa/caa was significant for the group of Simmental crossbreeds among healthy cattle. The allele and genotype distribution of the other polymorphisms was not significantly different among groups of healthy and BSE-affected cattle. The possible influence of a silent mutation on expression of the gene is not clearly determined and needs further investigations.

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4

Pandey, Krishna K., James P. Snyder, Dennis C. Liotta, and Djamaladdin G. Musaev. "Computational Studies of Transition Metal Selectivity of Octapeptide Repeat Region of Prion Protein (PrP)." Journal of Physical Chemistry B 114, no. 2 (January 21, 2010): 1127–35. http://dx.doi.org/10.1021/jp909945e.

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5

Perera, W. S. S., and N. M. Hooper. "Role of the octapeptide repeat region of the prion protein in copper homeostasis and endocytosis." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A347. http://dx.doi.org/10.1042/bst028a347c.

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6

Shiraishi, Noriyuki, Yuriko Ohta, and Morimitsu Nishikimi. "The Octapeptide Repeat Region of Prion Protein Binds Cu(II) in the Redox-Inactive State." Biochemical and Biophysical Research Communications 267, no. 1 (January 2000): 398–402. http://dx.doi.org/10.1006/bbrc.1999.1944.

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7

Das, Nandita Rani, Hironori Miyata, Hideyuki Hara, Junji Chida, Keiji Uchiyama, Kentaro Masujin, Hitomi Watanabe, Gen Kondoh, and Suehiro Sakaguchi. "The N-Terminal Polybasic Region of Prion Protein Is Crucial in Prion Pathogenesis Independently of the Octapeptide Repeat Region." Molecular Neurobiology 57, no. 2 (November 9, 2019): 1203–16. http://dx.doi.org/10.1007/s12035-019-01804-5.

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8

Flechsig, Eckhard, Doron Shmerling, Ivan Hegyi, Alex J. Raeber, Marek Fischer, Antonio Cozzio, Christian von Mering, Adriano Aguzzi, and Charles Weissmann. "Prion Protein Devoid of the Octapeptide Repeat Region Restores Susceptibility to Scrapie in PrP Knockout Mice." Neuron 27, no. 2 (August 2000): 399–408. http://dx.doi.org/10.1016/s0896-6273(00)00046-5.

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9

Sakudo, Akikazu, Deug-chan Lee, Takuya Nishimura, Shuming Li, Shoutaro Tsuji, Toyoo Nakamura, Yoshitsugu Matsumoto, et al. "Octapeptide repeat region and N-terminal half of hydrophobic region of prion protein (PrP) mediate PrP-dependent activation of superoxide dismutase." Biochemical and Biophysical Research Communications 326, no. 3 (January 2005): 600–606. http://dx.doi.org/10.1016/j.bbrc.2004.11.092.

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10

BROWN, David R., Boon-Seng WONG, Farida HAFIZ, Christine CLIVE, Stephen J. HASWELL, and Ian M. JONES. "Normal prion protein has an activity like that of superoxide dismutase." Biochemical Journal 344, no. 1 (November 8, 1999): 1–5. http://dx.doi.org/10.1042/bj3440001.

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We show here that mouse prion protein (PrPC) either as recombinant protein or immunoprecipitated from brain tissue has superoxide dismutase (SOD) activity. SOD activity was also associated with recombinant chicken PrPC confirming the evolutionary conserved phenotype suggested by sequence similarity. Acquisition of copper by PrPC during protein folding endowed SOD activity on the protein but the addition of copper following refolding did not. PrPC dependent SOD activity was abolished by deletion of the octapeptide-repeat region involved in copper binding. These results describe an enzymic function for PrPC consistent with its cellular distribution and suggest it has a direct role in cellular resistance to oxidative stress.

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