Identification of Distinct Amino Acid Composition of Human Cruciform Binding Proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F19%3AA20020ZY" target="_blank" >RIV/61988987:17310/19:A20020ZY - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/19:00510902

Výsledek na webu

<a href="https://link.springer.com/article/10.1134%2FS0026893319010023" target="_blank" >https://link.springer.com/article/10.1134%2FS0026893319010023</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1134/S0026893319010023" target="_blank" >10.1134/S0026893319010023</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Identification of Distinct Amino Acid Composition of Human Cruciform Binding Proteins

Popis výsledku v původním jazyce

Cruciform structures are preferential targets for many architectural and regulatory proteins, as well as a number of DNA binding proteins with weak sequence specificity. Some of these proteins are also capable of inducing the formation of cruciform structures upon DNA binding. In this paper we analyzed the amino acid composition of eighteen cruciform binding proteins of Homo sapiens. Comparison with general amino acid frequencies in all human proteins revealed unique differences, with notable enrichment for lysine and serine and/or depletion for alanine, glycine, glutamine, arginine, tyrosine and tryptophan residues. Based on bootstrap resampling and fuzzy cluster analysis, multiple molecular mechanisms of interaction with cruciform DNA structures could be suggested, including those involved in DNA repair, transcription and chromatin regulation. The proteins DEK, HMGB1 and TOP1 in particular formed a very distinctive group. Nonetheless, a strong interaction network connecting nearly all the cruciform binding proteins studied was demonstrated. Data reported here will be very useful for future prediction of new cruciform binding proteins or even construction of predictive tool/web-based application.

Název v anglickém jazyce

Identification of Distinct Amino Acid Composition of Human Cruciform Binding Proteins

Popis výsledku anglicky

Cruciform structures are preferential targets for many architectural and regulatory proteins, as well as a number of DNA binding proteins with weak sequence specificity. Some of these proteins are also capable of inducing the formation of cruciform structures upon DNA binding. In this paper we analyzed the amino acid composition of eighteen cruciform binding proteins of Homo sapiens. Comparison with general amino acid frequencies in all human proteins revealed unique differences, with notable enrichment for lysine and serine and/or depletion for alanine, glycine, glutamine, arginine, tyrosine and tryptophan residues. Based on bootstrap resampling and fuzzy cluster analysis, multiple molecular mechanisms of interaction with cruciform DNA structures could be suggested, including those involved in DNA repair, transcription and chromatin regulation. The proteins DEK, HMGB1 and TOP1 in particular formed a very distinctive group. Nonetheless, a strong interaction network connecting nearly all the cruciform binding proteins studied was demonstrated. Data reported here will be very useful for future prediction of new cruciform binding proteins or even construction of predictive tool/web-based application.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Biology

ISSN

0026-8933

e-ISSN

—

Svazek periodika

53

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

RU - Ruská federace

Počet stran výsledku

9

Strana od-do

97-106

Kód UT WoS článku

000468512300012

EID výsledku v databázi Scopus

—