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Coupled interaction of hMutSalpha nu...

Duke University.

Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities.
Author:	Martik, Diana.
Description:	137 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2923.
Notes:	Supervisor: Paul Modrich.
Contained By:	Dissertation Abstracts International65-06B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3136830
ISBN:	0496840266

Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities.
Martik, Diana.

Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities. - 137 p.

Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2923.

Thesis (Ph.D.)--Duke University, 2003.

As each subunit of hMutSalpha contains a highly conserved nucleotide binding motif that is associated with ATPase activity, the protein may exist in a number of potential nucleotide-bound conformations. Filter binding and fluorescence assay were utilized to define the possible states of nucleotide occupancy that the protein is likely to adopt. These studies found that while the protein has similar affinity for ADP and nonhydrolyzable ATP analogues, the two nucleotide binding centers in the hMutSalpha heterodimer display distinct specificities for ADP and ATP. Di- and triphosphate were further shown to simultaneously bind to hMutSalpha, thus suggesting the possibility of alternating site reactivity.

ISBN: 0496840266Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities.
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100 0 $a Martik, Diana. $3 227927
245 1 0 $a Coupled interaction of hMutSalpha nucleotide and DNA mismatch binding activities.
300 $a 137 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2923.
500 $a Supervisor: Paul Modrich.
502 $a Thesis (Ph.D.)--Duke University, 2003.
520 # $a As each subunit of hMutSalpha contains a highly conserved nucleotide binding motif that is associated with ATPase activity, the protein may exist in a number of potential nucleotide-bound conformations. Filter binding and fluorescence assay were utilized to define the possible states of nucleotide occupancy that the protein is likely to adopt. These studies found that while the protein has similar affinity for ADP and nonhydrolyzable ATP analogues, the two nucleotide binding centers in the hMutSalpha heterodimer display distinct specificities for ADP and ATP. Di- and triphosphate were further shown to simultaneously bind to hMutSalpha, thus suggesting the possibility of alternating site reactivity.
520 # $a Filter binding assay also demonstrated that occupancy of the hMutSalpha•nucleotide complex is modulated by heteroduplex cofactor, as release of the ATP analogue, AMPPNP, was stimulated in a mismatch-dependent manner. The coupling of hMutSalpha nucleotide and DNA binding activities was further clarified by surface plasmon resonance spectroscopy. hMutSalpha retained mismatch specificity in the presence of adenine nucleotides, but the occupancy of the nucleotide binding centers differentially modulated.
520 # $a The participation of hMutSalpha (hMSH2•hMSH6) in DNA mismatch repair requires both its mismatch binding and ATPase activities. The manner by which these biochemical activities are coupled was investigated in terms of the modulatory effects of nucleotide cofactor on hMutSalpha-DNA interaction. A model for hMutSalpha function in mismatch recognition and coordination of later steps in the repair reaction is presented.
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650 # 0 $a Biology, Molecular. $3 226919
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710 0 # $a Duke University. $3 226880
773 0 # $g 65-06B. $t Dissertation Abstracts International
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790 1 0 $a Modrich, Paul, $e advisor
791 $a Ph.D.
792 $a 2003
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