TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 31, Issue of July 30, pp. 21659 –21664, 1999 © 1999 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Dissociation of Mismatch Recognition and ATPase Activity by hMSH2-hMSH3* (Received for publication, March 10, 1999, and in revised form, May 12, 1999) Teresa Wilson, Shawn Guerrette, and Richard Fishel‡ From the Genetics and Molecular Biology Program, Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107 MSH2-MSH3 directs the repair of insertion/deletion may “slip,” forming insertion/deletion loops (IDL) that would loops of up to 13 nucleotides in vivo and in vitro.To then result in the lengthening or shortening of these sequences examine the biochemical basis of this repair specificity, if left unrepaired (17). The MMR pathway appears largely we characterized the mispair binding and ATPase activ- responsible for the repair of IDLs as well as simple mismatched ity of hMSH2-hMSH3. The ATPase was found to be reg- nucleotides that presumably arise as a result of misincorpora- ulated by a mismatch-stimulated ADP 3 ATP exchange, tion errors during DNA replication (for review see Ref. 15). which induces a conformational transition by the pro- Interestingly, 
TI - Dissociation of Mismatch Recognition and ATPase Activity by hMSH2-hMSH3
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.274.31.21659
DA - 1999-07-01
UR - https://www.deepdyve.com/lp/unpaywall/dissociation-of-mismatch-recognition-and-atpase-activity-by-hmsh2-cD7s3SFwmV
DP - DeepDyve
ER -