The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand

<p>Abstract</p> <p>Background</p> <p>We study the usage of specific peptide platforms in protein composition. Using the pentapeptide as a unit of length, we find that in the universal proteome many pentapeptides are heavily repeated (even thousands of times), whereas so...

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Main Authors: Bickis Mik, Trost Brett, Fasano Candida, Novello Giuseppe, Capone Giovanni, Kusalik Anthony, Kanduc Darja
Format: Article
Language:English
Published: BMC 2010-07-01
Series:BMC Bioinformatics
Online Access:http://www.biomedcentral.com/1471-2105/11/383
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spelling doaj-36ec79bd9bee4a79bc426b05bd75bcb12020-11-24T23:47:09ZengBMCBMC Bioinformatics1471-21052010-07-0111138310.1186/1471-2105-11-383The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strandBickis MikTrost BrettFasano CandidaNovello GiuseppeCapone GiovanniKusalik AnthonyKanduc Darja<p>Abstract</p> <p>Background</p> <p>We study the usage of specific peptide platforms in protein composition. Using the pentapeptide as a unit of length, we find that in the universal proteome many pentapeptides are heavily repeated (even thousands of times), whereas some are quite rare, and a small number do not appear at all. To understand the physico-chemical-biological basis underlying peptide usage at the proteomic level, in this study we analyse the energetic costs for the synthesis of rare and never-expressed versus frequent pentapeptides. In addition, we explore residue bulkiness, hydrophobicity, and codon number as factors able to modulate specific peptide frequencies. Then, the possible influence of amino acid composition is investigated in zero- and high-frequency pentapeptide sets by analysing the frequencies of the corresponding inverse-sequence pentapeptides. As a final step, we analyse the pentadecamer oligodeoxynucleotide sequences corresponding to the never-expressed pentapeptides.</p> <p>Results</p> <p>We find that only DNA context-dependent constraints (such as oligodeoxynucleotide sequence location in the minus strand, introns, pseudogenes, frameshifts, etc.) provide a coherent mechanistic platform to explain the occurrence of never-expressed versus frequent pentapeptides in the protein world.</p> <p>Conclusions</p> <p>This study is of importance in cell biology. Indeed, the rarity (or lack of expression) of specific 5-mer peptide modules implies the rarity (or lack of expression) of the corresponding <it>n</it>-mer peptide sequences (with <it>n </it>< 5), so possibly modulating protein compositional trends. Moreover the data might further our understanding of the role exerted by rare pentapeptide modules as critical biological effectors in protein-protein interactions.</p> http://www.biomedcentral.com/1471-2105/11/383
collection DOAJ
language English
format Article
sources DOAJ
author Bickis Mik
Trost Brett
Fasano Candida
Novello Giuseppe
Capone Giovanni
Kusalik Anthony
Kanduc Darja
spellingShingle Bickis Mik
Trost Brett
Fasano Candida
Novello Giuseppe
Capone Giovanni
Kusalik Anthony
Kanduc Darja
The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
BMC Bioinformatics
author_facet Bickis Mik
Trost Brett
Fasano Candida
Novello Giuseppe
Capone Giovanni
Kusalik Anthony
Kanduc Darja
author_sort Bickis Mik
title The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
title_short The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
title_full The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
title_fullStr The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
title_full_unstemmed The oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
title_sort oligodeoxynucleotide sequences corresponding to never-expressed peptide motifs are mainly located in the non-coding strand
publisher BMC
series BMC Bioinformatics
issn 1471-2105
publishDate 2010-07-01
description <p>Abstract</p> <p>Background</p> <p>We study the usage of specific peptide platforms in protein composition. Using the pentapeptide as a unit of length, we find that in the universal proteome many pentapeptides are heavily repeated (even thousands of times), whereas some are quite rare, and a small number do not appear at all. To understand the physico-chemical-biological basis underlying peptide usage at the proteomic level, in this study we analyse the energetic costs for the synthesis of rare and never-expressed versus frequent pentapeptides. In addition, we explore residue bulkiness, hydrophobicity, and codon number as factors able to modulate specific peptide frequencies. Then, the possible influence of amino acid composition is investigated in zero- and high-frequency pentapeptide sets by analysing the frequencies of the corresponding inverse-sequence pentapeptides. As a final step, we analyse the pentadecamer oligodeoxynucleotide sequences corresponding to the never-expressed pentapeptides.</p> <p>Results</p> <p>We find that only DNA context-dependent constraints (such as oligodeoxynucleotide sequence location in the minus strand, introns, pseudogenes, frameshifts, etc.) provide a coherent mechanistic platform to explain the occurrence of never-expressed versus frequent pentapeptides in the protein world.</p> <p>Conclusions</p> <p>This study is of importance in cell biology. Indeed, the rarity (or lack of expression) of specific 5-mer peptide modules implies the rarity (or lack of expression) of the corresponding <it>n</it>-mer peptide sequences (with <it>n </it>< 5), so possibly modulating protein compositional trends. Moreover the data might further our understanding of the role exerted by rare pentapeptide modules as critical biological effectors in protein-protein interactions.</p>
url http://www.biomedcentral.com/1471-2105/11/383
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