The role of the zinc motif in sequence recognition by DNA primases

Takahiro Kusakabe, Charles C. Richardson

研究成果: ジャーナルへの寄稿記事

54 引用 (Scopus)

抄録

The DNA primase of bacteriophage T7 has a zinc-binding motif that is essential for the recognition of the sequence 3'-CTG-5'. The T7 primase also catalyzes helicase activity, a reaction coupled to nucleotide hydrolysis. We have replaced the zinc motif of the T7 primase with those found in the gene 61 primase of phage T4 and the DnaG primase of Escherichia coli. The T4 and E. coli primases recognize the sequences 3'-T(C/T)G-5' and 3'-GTC-5', respectively. Both chimeric proteins can partially replace T7 primase in vivo. The two chimeric primases catalyze the synthesis of oligoribonucleotides albeit at a reduced rate and DNA dependent dTTPase activity is reduced by 3-10-fold. Both chimeric proteins recognize 3'- (A/G)CG-5' sites on single-stranded DNA, sites that differ from those recognized by the T7, T4, or E. coli primases, indicating that the zinc motif is only one determinant in site-specific recognition.

元の言語英語
ページ(範囲)19563-19570
ページ数8
ジャーナルJournal of Biological Chemistry
271
発行部数32
DOI
出版物ステータス出版済み - 8 27 1996
外部発表Yes

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DNA Primase
Zinc
Escherichia coli
Bacteriophages
Oligoribonucleotides
Bacteriophage T7
Bacteriophage T4
Single-Stranded DNA
Hydrolysis
Proteins
Nucleotides
Genes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

The role of the zinc motif in sequence recognition by DNA primases. / Kusakabe, Takahiro; Richardson, Charles C.

:: Journal of Biological Chemistry, 巻 271, 番号 32, 27.08.1996, p. 19563-19570.

研究成果: ジャーナルへの寄稿記事

Kusakabe, Takahiro ; Richardson, Charles C. / The role of the zinc motif in sequence recognition by DNA primases. :: Journal of Biological Chemistry. 1996 ; 巻 271, 番号 32. pp. 19563-19570.
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