NDLI: Biochemical Characterization of the WRN-1 RecQ Helicase of Caenorhabditis elegans †

Content Provider	PubMed Central
Author	Hyun, Moonjung Bohr, Vilhelm A. Ahn, Byungchan
Abstract	The highly conserved RecQ helicases are essential for the maintenance of genomic stability. Werner syndrome protein, WRN, is one of five human RecQ helicase homologues, and a deficiency of the protein causes a hereditary premature aging disorder that is characterized by genomic instability. A WRN orthologue, wrn-1 lacking the exonuclease domain, has been identified in the nematode Caenorhabditis elegans. wrn-1(RNAi) in C. elegans has a shortened life span, increased sensitivity to DNA damage, and accelerated aging phenotypes. However, little is known about its enzymatic activity. We purified the recombinant C. elegans WRN-1 protein (CeWRN-1) and then investigated its substrate specificity in vitro to improve our understanding of its function in vivo. We found that CeWRN-1 is an ATP-dependent 3′—5′ helicase capable of unwinding a variety of DNA structures such as forked duplexes, Holliday junctions, bubble substrates, D-loops, and flap duplexes, and 3′-tailed duplex substrates. Distinctly, CeWRN-1 is able to unwind a long forked duplex compared to human WRN. Furthermore, CeWRN-1 helicase activity on a long DNA duplex is stimulated by C. elegans replication protein A (CeRPA) that is shown to interact with CeWRN-1 by a dot blot. The ability of CeWRN-1 to unwind these DNA structures may improve the access for DNA repair and replication proteins that are important for preventing the accumulation of abnormal structures, contributing to genomic stability.
Related Links	http://dx.doi.org/10.1021/bi800197m
Ending Page	7593
Page Count	11
Starting Page	7583
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	28
Volume Number	47
Language	English
Publisher Date	2008-07-01
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

Sl.	Authority	Responsibilities	Communication Details
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
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

RecQ Helicase Somatic Alterations in Cancer

Down regulation of miR-124 in both Werner syndrome DNA helicase mutant mice and mutant Caenorhabditis elegans wrn-1 reveals the importance of this microRNA in accelerated aging

Characterization of Biochemical Properties of Bacillus subtilis RecQ Helicase

Biochemical and molecular characterization of two cytidine deaminases in the nematode Caenorhabditis elegans.

Genetic Suppressors of Caenorhabditis elegans pha-4/FoxA Identify the Predicted AAA Helicase ruvb-1/RuvB

Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans.

The interaction site of Flap Endonuclease-1 with WRN helicase suggests a coordination of WRN and PCNA

Biochemical characterization of Caenorhabditis elegans UBC-1: self-association and auto-ubiquitination of a RAD6-like ubiquitin-conjugating enzyme in vitro.

The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest

Biochemical Characterization of the WRN-1 RecQ Helicase of Caenorhabditis elegans †

Similar Documents

RecQ Helicase Somatic Alterations in Cancer

Down regulation of miR-124 in both Werner syndrome DNA helicase mutant mice and mutant Caenorhabditis elegans wrn-1 reveals the importance of this microRNA in accelerated aging

Characterization of Biochemical Properties of Bacillus subtilis RecQ Helicase

Biochemical and molecular characterization of two cytidine deaminases in the nematode Caenorhabditis elegans.

Genetic Suppressors of Caenorhabditis elegans pha-4/FoxA Identify the Predicted AAA Helicase ruvb-1/RuvB

Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans.

The interaction site of Flap Endonuclease-1 with WRN helicase suggests a coordination of WRN and PCNA

Biochemical characterization of Caenorhabditis elegans UBC-1: self-association and auto-ubiquitination of a RAD6-like ubiquitin-conjugating enzyme in vitro.

The RecQ helicase WRN is required for normal replication fork progression after DNA damage or replication fork arrest

Biochemical Characterization of the WRN-1 RecQ Helicase of Caenorhabditis elegans †