NDLI: Structure of a Longitudinal Actin Dimer Assembled by Tandem W Domains – Implications for Actin Filament Nucleation

Content Provider	PubMed Central
Author	Rebowski, Grzegorz Suk, Namgoong Boczkowska, Malgorzata Leavis, Paul C. Navaza, Jorge Dominguez, Roberto
Copyright Year	2010
Abstract	Actin filament nucleators initiate polymerization in cells in a regulated manner. A common architecture among these molecules consists of tandem W domains that recruit three to four actin subunits to form a polymerization nucleus. We describe a low-resolution crystal structure of an actin dimer assembled by tandem W domains, where the first W domain is crosslinked to Cys-374 of the actin subunit bound to it, whereas the last W domain is followed by the C-terminal pointed end-capping helix of Tβ4. While the arrangement of actin subunits in the dimer resembles that of a long-pitch helix of the actin filament, important differences are observed. These differences result from steric hindrance of the W domain with inter-subunit contacts in the actin filament. We also determined the structure of the first W domain of Vibrio parahaemolyticus VopL crosslinked to actin Cys-374, and show it to be nearly identical to non-crosslinked W-actin structures. This result validates the use of crosslinking as a tool for the study of actin nucleation complexes, whose natural tendency to polymerize interferes with most structural methods. Combined with a biochemical analysis of nucleation, the structures may explain why nucleators based on tandem W domains with short inter-W linkers have relatively weak activity, cannot stay bound to filaments after nucleation, and are unlikely to influence filament elongation. The findings may also explain why Nucleation Promoting Factors of the Arp2/3 complex, which are related to tandem W domain nucleators, are ejected from branch junctions after nucleation. We finally show that the simple addition of the C-terminal pointed end-capping helix of Tβ4 to tandem W domains can change their activity from actin filament nucleation to monomer sequestration.
Related Links	http://dx.doi.org/10.1016/j.jmb.2010.08.040
Ending Page	23
Page Count	13
Starting Page	11
File Format	PDF
ISSN	00222836
e-ISSN	10898638
Journal	Journal of molecular biology
Issue Number	1
Volume Number	403
Language	English
Publisher Date	2010-10-01
Access Restriction	Open
Subject Keyword	Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biophysics

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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