Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder
AbstractAn 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
Share & Cite This Article
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.
Machulin A, Deryusheva E, Lobanov M, Galzitskaya O. Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder. International Journal of Molecular Sciences. 2019; 20(10):2377.Chicago/Turabian Style
Machulin, Andrey; Deryusheva, Evgenia; Lobanov, Mikhail; Galzitskaya, Oxana. 2019. "Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder." Int. J. Mol. Sci. 20, no. 10: 2377.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.