Flexibility of the linker between the domains of DNA methyltransferase SsoII revealed by small-angle X-ray scattering: implications for transcription regulation in SsoII restriction-modification system

Konarev, P.V.; Kachalova, G.S.; Ryazanova, A.Y.; Kubareva, E.A.; Karyagina, A.S.; Bartunik, H.D.; Svergun, D.I.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Web of Science, Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 20 мая 2014 г.

Авторы: Konarev P.V., Kachalova G.S., Ryazanova A.Yu, Kubareva E.A., Karyagina A.S., Bartunik H.D., Svergun D.I.
Журнал: PLoS ONE
Том: 9
Номер: 4
Год издания: 2014
Издательство: Public Library of Science
Местоположение издательства: United States
Первая страница: e93453
DOI: 10.1371/journal.pone.0093453
Аннотация: (Cytosine-5)-DNA methyltransferase SsoII (M.SsoII) consists of a methyltransferase domain (residues 72–379) and an N-terminal region (residues 1–71) which regulates transcription in SsoII restriction–modification system. Small-angle X-ray scattering (SAXS) is employed here to study the low resolution structure of M.SsoII and its complex with DNA containing the methylation site. The shapes reconstructed ab initio from the SAXS data reveal two distinct protein domains of unequal size. The larger domain matches the crystallographic structure of a homologous DNA methyltransferase HhaI (M.HhaI), and the cleft in this domain is occupied by DNA in the model of the complex reconstructed from the SAXS data. This larger domain can thus be identified as the methyltransferase domain whereas the other domain represents the N-terminal region. Нomology modeling of the M.SsoII structure is performed by using the model of M.HhaI for the methyltransferase domain and representing the N-terminal region either as a flexible chain of dummy residues or as a rigid structure of a homologous protein (phage 434 repressor) connected to the methyltransferase domain by a short flexible linker. Both models are compatible with the SAXS data and demonstrate high mobility of the N-terminal region. The linker flexibility might play an important role in the function of M.SsoII as a transcription factor.
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Flexibility of the linker between the domains of DNA methyltransferase SsoII revealed by small-angle X-ray scattering: implications for transcription regulation in SsoII restriction-modification systemстатья

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