Self-organization of parS centromeres by the ParB CTP hydrolase-Reference-Cited by-同舟云学术

Self-organization of parS centromeres by the ParB CTP hydrolase

Published:2019-11-29 Issue:6469 Volume:366 Page:1129-1133
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Soh Young-Min¹^ORCID,Davidson Iain Finley²^ORCID,Zamuner Stefano³,Basquin Jérôme⁴,Bock Florian Patrick¹^ORCID,Taschner Michael¹^ORCID,Veening Jan-Willem¹^ORCID,De Los Rios Paolo³,Peters Jan-Michael²^ORCID,Gruber Stephan¹^ORCID

Affiliation:

1. Department of Fundamental Microbiology (DMF), Faculty of Biology and Medicine (FBM), University of Lausanne (UNIL), Lausanne, Switzerland.

2. Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC) and Medical University of Vienna, Vienna, Austria.

3. Laboratory of Statistical Biophysics, Institute of Physics, School of Basic Sciences and Institute of Bioengineering, School of Life Sciences, École Polytechnique Féderale de Lausanne (EPFL), Lausanne, Switzerland.

4. Structural Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.

Abstract

CTP hydrolysis organizes chromosomes The bacterial DNA parS centromere recruits the ParB protein to the bacterial chromosome. Soh et al. found that the widespread family of ParB proteins not only bind DNA but also bind and hydrolyze cytidine triphosphate (CTP) (see the Perspective by Funnell). ParB CTP hydrolysis is stimulated by parS and regulates the spreading of ParB protein to the parS flanking regions, which is crucial for organizing the bacterial chromosome. The cytidine triphosphatase domain is conserved in a large variety of protein sequences, suggesting its potential roles in other cellular processes. Science , this issue p. 1129 ; see also p. 1072

Funder

H2020 European Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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