The beta subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits.-Reference-Cited by-同舟云学术

The beta subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits.

Published:1986-06 Issue:16 Volume:261 Page:7550-7557
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

LaDuca R J,Crute J J,McHenry C S,Bambara R A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference29 articles.

1. Isolation of Supercoiled Colicinogenic Factor E1 DNA Sensitive to Ribonuclease and Alkali

2. ATP activation of DNA polymerase III holoenzyme of Escherichia coli. I. ATP-dependent formation of an initiation complex with a primed template.

3. ATP activation of DNA polymerase III holoenzyme from Escherichia coli. II. Initiation complex: stoichiometry and reactivity.

4. Amplification of single-strand DNA binding protein in Escherichis coli

5. Excess beta subunit can bypass the ATP requirement for highly processive synthesis by the Escherichia coli DNA polymerase III holoenzyme.

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