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Title 

Mutagenesis of the positively charged conserved residues in the 5' exonuclease domain of Taq DNA polymerase

Authors 

Young Soo KimJoong Su KimYoung Hyun ParkChang Soo ChangSe Won SuhDae Sil Lee

Publisher 

Springer Verlag (Germany)

Issue Date 

1997

Citation 

Molecules and Cells, vol. 7, no. 4, pp. 468-472

Keywords 

Taq polymerasesite directed mutagenesisconserved sequenceMutagenesis, Site-Directed

Abstract 

Taq DNA polymerase from Thermus aquaticus has been shown to be very useful in the polymerase chain reaction method. Taq DNA polymerase has a domain at the amino terminus (residue 1 to 290) that has a 5′ exonuclease activity and a domain at the C-terminus that catalyzes polymerase reaction. Taq DNA polymerase is classified into the pol I family which is represented by E. coli DNA polymerase I. The alignment of amino acid sequences for the 5′ exonuclease domains of the pol I family DNA polymerases shows six highly conserved sequences called motifs A to F. Motif C contains three positively charged residues such as 74Arg, 82Lys and 85Arg which might be involved in catalysis. In order to understand the function of those residues, they are mutagenized to alanine. The 5′ exonucleolytic activities of those mutated 5′ exonucleases decreased by 80 to 90%, thereby implying that three positively charged residues play certain roles in the 5′ exonuclease catalysis.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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