A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- and P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4.-Reference-Cited by-同舟云学术

A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- and P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4.

Published:1992-06 Issue:18 Volume:267 Page:13062-13072
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Strack B,Lessl M,Calendar R,Lanka E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference84 articles.

1. An Escherichia coli cis-acting antiterminator sequence: The dnaG nut site

2. A sequence motif in many polymerases

3. A Transcribing Activity Induced by Satellite Phage P4

4. The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization.

5. Purification of the 56-kDa component of the bacteriophage T7 primase/helicase and characterization of its nucleoside 5′-triphosphatase activity.

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