Homepeptide Repeats: Implications for Protein Structure, Function and Evolution

Overview

Journal Genomics Proteomics Bioinformatics

Specialty Biology

Date 2012 Oct 23

PMID 23084777

Citations 5

Authors

Muthukumarasamy Uthayakumar

Bowdadu Benazir

Sanjeev Patra

Marthandan Kirti Vaishnavi

Manickam Gurusaran

Kanagarajan Sureka

Jeyaraman Jeyakanthan

Kanagaraj Sekar

Affiliations

Soon will be listed here.

Abstract

Analysis of protein sequences from Mycobacterium tuberculosis H37Rv (Mtb H37Rv) was performed to identify homopeptide repeat-containing proteins (HRCPs). Functional annotation of the HRCPs showed that they are preferentially involved in cellular metabolism. Furthermore, these homopeptide repeats might play some specific roles in protein-protein interaction. Repeat length differences among Bacteria, Archaea and Eukaryotes were calculated in order to identify the conservation of the repeats in these divergent kingdoms. From the results, it was evident that these repeats have a higher degree of conservation in Bacteria and Archaea than in Eukaryotes. In addition, there seems to be a direct correlation between the repeat length difference and the degree of divergence between the species. Our study supports the hypothesis that the presence of homopeptide repeats influences the rate of evolution of the protein sequences in which they are embedded. Thus, homopeptide repeat may have structural, functional and evolutionary implications on proteins.

Citing Articles

The relationship between protein domains and homopeptides in the proteome.

Wang Y, Yang H, Harrison P PeerJ. 2020; 8:e9940.

PMID: 33062426 PMC: 7534687. DOI: 10.7717/peerj.9940.

Identification and Analysis of Long Repeats of Proteins at the Domain Level.

Mary Rajathei D, Parthasarathy S, Selvaraj S Front Bioeng Biotechnol. 2019; 7:250.

PMID: 31649924 PMC: 6795024. DOI: 10.3389/fbioe.2019.00250.

Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias.

Barik S Heliyon. 2018; 3(12):e00492.

PMID: 29387823 PMC: 5772840. DOI: 10.1016/j.heliyon.2017.e00492.

PPS: A computing engine to find Palindromes in all Protein sequences.

Ahmed Z, Gurusaran M, Narayana P, Kumar K, Mohanapriya J, Vaishnavi M Bioinformation. 2014; 10(1):48-51.

PMID: 24516327 PMC: 3916820. DOI: 10.6026/97320630010048.

Search and analysis of identical reverse octapeptides in unrelated proteins.

Saravanan K, Selvaraj S Genomics Proteomics Bioinformatics. 2013; 11(2):114-21.

PMID: 23523652 PMC: 4357837. DOI: 10.1016/j.gpb.2012.11.005.

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