NDLI: Functional Residues on the Surface of the N-terminal domain of Yeast Pms1

Content Provider	PubMed Central
Author	Arana, Mercedes E. Holmes, Shannon F. Fortune, John M. Moon, Andrea F. Pedersen, Lars C. Kunkel, Thomas A.
Abstract	Saccharomyces cerevisiae MutLα is a heterodimer of Mlh1 and Pms1 that participates in DNA mismatch repair (MMR). Both proteins have weakly conserved C-terminal regions (CTD), with the CTD of Pms1 harboring an essential endonuclease activity. These proteins also have conserved N-terminal domains (NTD) that bind and hydrolyze ATP and bind to DNA. To better understand Pms1 functions and potential interactions with DNA and/or other proteins, we solved the 2.5Å crystal structure of yeast Pms1 (yPms1) NTD. The structure is similar to thehomologous NTDs of E. coli MutL and human PMS2, including the site involved in ATP binding and hydrolysis. The structure reveals a number of conserved, positively charged surface residues that do not interact with other residues in the NTD and are therefore candidates for interactions with DNA, with the CTD and/or with other proteins. When these were replaced with glutamate, several replacements resulted in yeast strains with elevated mutation rates. Two replacements also resulted in NTDs with decreased DNA binding affinity in vitro, suggesting that these residues contribute to DNA binding that is important for mismatch repair. Elevated mutation rates also resulted from surface residue replacements that did not affect DNA binding, suggesting that these conserved residues serve other functions, possibly involving interactions with other MMR proteins.
Related Links	http://dx.doi.org/10.1016/j.dnarep.2010.01.010
Ending Page	457
Page Count	10
Starting Page	448
File Format	PDF
ISSN	15687864
e-ISSN	15687856
Journal	DNA repair
Issue Number	4
Volume Number	9
Language	English
Publisher Date	2010-04-01
Access Restriction	Open
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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

Crystal Structure of the N-terminal Domain of the Yeast General Corepressor Tup1p and Its Functional Implications*

Functional Characterization of the N-terminal Domain of Subunit H (Vma13p) of the Yeast Vacuolar ATPase*

The N-terminal Domain of the Yeast Mitochondrial RNA Polymerase Regulates Multiple Steps of Transcription*

Yeast Mps1p Phosphorylates the Spindle Pole Component Spc110p in the N-terminal Domain *

Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG

Function and Subunit Interactions of the N-terminal Domain of Subunit a (Vph1p) of the Yeast V-ATPase*

Structural and Functional Separation of the N- and C-terminal Domains of the Yeast V-ATPase Subunit H*

Functional analysis of interaction sites on the N-terminal domain of clathrin heavy chain

Identification and Functional Characterization of an N-terminal Oligomerization Domain for Polycystin-2*

Functional Residues on the Surface of the N-terminal domain of Yeast Pms1

Similar Documents

Crystal Structure of the N-terminal Domain of the Yeast General Corepressor Tup1p and Its Functional Implications*

Functional Characterization of the N-terminal Domain of Subunit H (Vma13p) of the Yeast Vacuolar ATPase*

The N-terminal Domain of the Yeast Mitochondrial RNA Polymerase Regulates Multiple Steps of Transcription*

Yeast Mps1p Phosphorylates the Spindle Pole Component Spc110p in the N-terminal Domain *

Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG

Function and Subunit Interactions of the N-terminal Domain of Subunit a (Vph1p) of the Yeast V-ATPase*

Structural and Functional Separation of the N- and C-terminal Domains of the Yeast V-ATPase Subunit H*

Functional analysis of interaction sites on the N-terminal domain of clathrin heavy chain

Identification and Functional Characterization of an N-terminal Oligomerization Domain for Polycystin-2*

Functional Residues on the Surface of the N-terminal domain of Yeast Pms1