Literature DB >> 2786875

The 44P subunit of the T4 DNA polymerase accessory protein complex catalyzes ATP hydrolysis.

J Rush1, T C Lin, M Quinones, E K Spicer, I Douglas, K R Williams, W H Konigsberg.   

Abstract

The genes encoding all three T4 DNA polymerase accessory proteins have been cloned into overexpression plasmids. Induction of cells harboring these plasmids results in the synthesis of each accessory protein at levels that approach 10% of the total cellular protein. The solubility of the accessory proteins after induction at 42 degrees C ranges from about 60% to greater than 95%. A plasmid that allows overexpression of the 44P/62P complex has been manipulated further to overexpress selectively the 44P subunit without 62P, permitting us to assess how each subunit contributes to the properties of the 44P/62P complex. A comparison of 44P and 44P/62P by conventional hydrodynamic techniques shows that 44P forms a subcomplex nearly as large as the 44P/62P complex. In addition, 44P catalyzes DNA-dependent ATP hydrolysis with a specific activity similar to that of the 44P/62P ATPase. However, unlike the 44P/62P complex, the ATPase activity of 44P alone is only slightly stimulated by 45P. This suggests that one role of the 62P subunit is to facilitate a productive interaction of 44P and 45P.

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Year:  1989        PMID: 2786875

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  21 in total

1.  Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer.

Authors:  M A Trakselis; S C Alley; E Abel-Santos; S J Benkovic
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-17       Impact factor: 11.205

2.  Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells.

Authors:  M Chen; Z Q Pan; J Hurwitz
Journal:  Proc Natl Acad Sci U S A       Date:  1992-04-01       Impact factor: 11.205

3.  The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage.

Authors:  I Gordienko; W D Rupp
Journal:  EMBO J       Date:  1997-02-17       Impact factor: 11.598

4.  Divergence of a DNA replication gene cluster in the T4-related bacteriophage RB69.

Authors:  L S Yeh; T Hsu; J D Karam
Journal:  J Bacteriol       Date:  1998-04       Impact factor: 3.490

5.  UvrAB activity at a damaged DNA site: is unpaired DNA present?

Authors:  I Gordienko; W D Rupp
Journal:  EMBO J       Date:  1997-02-17       Impact factor: 11.598

6.  RNA primer-primase complexes serve as the signal for polymerase recycling and Okazaki fragment initiation in T4 phage DNA replication.

Authors:  Michelle M Spiering; Philip Hanoian; Swathi Gannavaram; Stephen J Benkovic
Journal:  Proc Natl Acad Sci U S A       Date:  2017-05-15       Impact factor: 11.205

Review 7.  Replication clamps and clamp loaders.

Authors:  Mark Hedglin; Ravindra Kumar; Stephen J Benkovic
Journal:  Cold Spring Harb Perspect Biol       Date:  2013-04-01       Impact factor: 10.005

8.  Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.

Authors:  Jing Fang; Philip Nevin; Visvaldas Kairys; Česlovas Venclovas; John R Engen; Penny J Beuning
Journal:  Structure       Date:  2014-03-06       Impact factor: 5.006

9.  Efficiency and frequency of translational coupling between the bacteriophage T4 clamp loader genes.

Authors:  M Y Torgov; D M Janzen; M K Reddy
Journal:  J Bacteriol       Date:  1998-09       Impact factor: 3.490

10.  Multiple ATP binding is required to stabilize the "activated" (clamp open) clamp loader of the T4 DNA replication complex.

Authors:  Paola Pietroni; Peter H von Hippel
Journal:  J Biol Chem       Date:  2008-08-01       Impact factor: 5.157

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