Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.

Proline is an anomalous amino acid. Its nitrogen atom is covalently locked within a ring, thus it is the only proteinogenic amino acid with a constrained phi angle. Sequences of three consecutive prolines can fold into polyproline helices, structures that join alpha helices and beta pleats as archit...

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Autores principales:	Alexander A Morgan, Edward Rubenstein
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e1409044fc1f4bc09326a079c6907427
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spelling	oai:doaj.org-article:e1409044fc1f4bc09326a079c69074272021-11-18T07:59:50ZProline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.1932-620310.1371/journal.pone.0053785https://doaj.org/article/e1409044fc1f4bc09326a079c69074272013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23372670/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Proline is an anomalous amino acid. Its nitrogen atom is covalently locked within a ring, thus it is the only proteinogenic amino acid with a constrained phi angle. Sequences of three consecutive prolines can fold into polyproline helices, structures that join alpha helices and beta pleats as architectural motifs in protein configuration. Triproline helices are participants in protein-protein signaling interactions. Longer spans of repeat prolines also occur, containing as many as 27 consecutive proline residues. Little is known about the frequency, positioning, and functional significance of these proline sequences. Therefore we have undertaken a systematic bioinformatics study of proline residues in proteins. We analyzed the distribution and frequency of 687,434 proline residues among 18,666 human proteins, identifying single residues, dimers, trimers, and longer repeats. Proline accounts for 6.3% of the 10,882,808 protein amino acids. Of all proline residues, 4.4% are in trimers or longer spans. We detected patterns that influence function based on proline location, spacing, and concentration. We propose a classification based on proline-rich, polyproline-rich, and proline-poor status. Whereas singlet proline residues are often found in proteins that display recurring architectural patterns, trimers or longer proline sequences tend be associated with the absence of repetitive structural motifs. Spans of 6 or more are associated with DNA/RNA processing, actin, and developmental processes. We also suggest a role for proline in Kruppel-type zinc finger protein control of DNA expression, and in the nucleation and translocation of actin by the formin complex.Alexander A MorganEdward RubensteinPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e53785 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alexander A Morgan Edward Rubenstein Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
description	Proline is an anomalous amino acid. Its nitrogen atom is covalently locked within a ring, thus it is the only proteinogenic amino acid with a constrained phi angle. Sequences of three consecutive prolines can fold into polyproline helices, structures that join alpha helices and beta pleats as architectural motifs in protein configuration. Triproline helices are participants in protein-protein signaling interactions. Longer spans of repeat prolines also occur, containing as many as 27 consecutive proline residues. Little is known about the frequency, positioning, and functional significance of these proline sequences. Therefore we have undertaken a systematic bioinformatics study of proline residues in proteins. We analyzed the distribution and frequency of 687,434 proline residues among 18,666 human proteins, identifying single residues, dimers, trimers, and longer repeats. Proline accounts for 6.3% of the 10,882,808 protein amino acids. Of all proline residues, 4.4% are in trimers or longer spans. We detected patterns that influence function based on proline location, spacing, and concentration. We propose a classification based on proline-rich, polyproline-rich, and proline-poor status. Whereas singlet proline residues are often found in proteins that display recurring architectural patterns, trimers or longer proline sequences tend be associated with the absence of repetitive structural motifs. Spans of 6 or more are associated with DNA/RNA processing, actin, and developmental processes. We also suggest a role for proline in Kruppel-type zinc finger protein control of DNA expression, and in the nucleation and translocation of actin by the formin complex.
format	article
author	Alexander A Morgan Edward Rubenstein
author_facet	Alexander A Morgan Edward Rubenstein
author_sort	Alexander A Morgan
title	Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
title_short	Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
title_full	Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
title_fullStr	Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
title_full_unstemmed	Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
title_sort	proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e1409044fc1f4bc09326a079c6907427
work_keys_str_mv	AT alexanderamorgan prolinethedistributionfrequencypositioningandcommonfunctionalrolesofprolineandpolyprolinesequencesinthehumanproteome AT edwardrubenstein prolinethedistributionfrequencypositioningandcommonfunctionalrolesofprolineandpolyprolinesequencesinthehumanproteome
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Proline: the distribution, frequency, positioning, and common functional roles of proline and polyproline sequences in the human proteome.

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