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Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder

1
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia
2
Institute for Biological Instrumentation, Federal Research Center “Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia
3
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(10), 2377; https://doi.org/10.3390/ijms20102377
Received: 9 April 2019 / Revised: 6 May 2019 / Accepted: 10 May 2019 / Published: 14 May 2019
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Abstract

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. View Full-Text
Keywords: ribosomal proteins S1; structural domains; intrinsically flexibility; FoldUnfold program; IsUnstruct program ribosomal proteins S1; structural domains; intrinsically flexibility; FoldUnfold program; IsUnstruct program
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Machulin, A.; Deryusheva, E.; Lobanov, M.; Galzitskaya, O. Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder. Int. J. Mol. Sci. 2019, 20, 2377.

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