Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder.
FoldUnfold program
IsUnstruct program
intrinsically flexibility
ribosomal proteins S1
structural domains
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
14 May 2019
14 May 2019
Historique:
received:
09
04
2019
revised:
06
05
2019
accepted:
10
05
2019
entrez:
17
5
2019
pubmed:
17
5
2019
medline:
27
8
2019
Statut:
epublish
Résumé
An important feature of ribosomal S1 proteins is multiple copies of structural domains in bacteria, the number of which changes in a strictly limited range from one to six. For S1 proteins, little is known about the contribution of flexible regions to protein domain function. We exhaustively studied a tendency for intrinsic disorder and flexibility within and between structural domains for all available UniProt S1 sequences. Using charge-hydrophobicity plot cumulative distribution function (CH-CDF) analysis we classified 53% of S1 proteins as ordered proteins; the remaining proteins were related to molten globule state. S1 proteins are characterized by an equal ratio of regions connecting the secondary structure within and between structural domains, which indicates a similar organization of separate S1 domains and multi-domain S1 proteins. According to the FoldUnfold and IsUnstruct programs, in the multi-domain proteins, relatively short flexible or disordered regions are predominant. The lowest percentage of flexibility is in the central parts of multi-domain proteins. Our results suggest that the ratio of flexibility in the separate domains is related to their roles in the activity and functionality of S1: a more stable and compact central part in the multi-domain proteins is vital for RNA interaction, terminals domains are important for other functions.
Identifiants
pubmed: 31091666
pii: ijms20102377
doi: 10.3390/ijms20102377
pmc: PMC6566611
pii:
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Ribosomal Proteins
0
ribosomal protein S1
0
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Russian Science Foundation
ID : 18-14-00321
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