Tracking Sliding Clamp Opening and Closing during Bacteriophage T4 DNA Polymerase Holoenzyme Assembly†

Biochemistry ◽  
2000 ◽  
Vol 39 (11) ◽  
pp. 3076-3090 ◽  
Author(s):  
Stephen C. Alley ◽  
Ernesto Abel-Santos ◽  
Stephen J. Benkovic
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Sliding Clamp ◽  
Opening And Closing

The Kinetic Mechanism of Formation of the Bacteriophage T4 DNA Polymerase Sliding Clamp

1996 ◽  
Vol 264 (3) ◽  
pp. 440-452 ◽  
Author(s):  
Mark C. Young ◽  
Steven E. Weitzel ◽  
Peter H. von Hippel
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Kinetic Mechanism ◽  
Mechanism Of Formation ◽  
Sliding Clamp

scholarly journals The Carboxyl Terminus of the Bacteriophage T4 DNA Polymerase Contacts Its Sliding Clamp at the Subunit Interface

1999 ◽  
Vol 274 (35) ◽  
pp. 24485-24489 ◽  
Author(s):  
Stephen C. Alley ◽  
A. Daniel Jones ◽  
Patrice Soumillion ◽  
Stephen J. Benkovic
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Carboxyl Terminus ◽  
Sliding Clamp ◽  
Subunit Interface

scholarly journals Structural Analyses of gp45 Sliding Clamp Interactions during Assembly of the Bacteriophage T4 DNA Polymerase Holoenzyme

1997 ◽  
Vol 272 (50) ◽  
pp. 31685-31692 ◽  
Author(s):  
Gary J. Latham ◽  
Daniel J. Bacheller ◽  
Paola Pietroni ◽  
Peter H. von Hippel
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Sliding Clamp

scholarly journals Structural Analyses of gp45 Sliding Clamp Interactions during Assembly of the Bacteriophage T4 DNA Polymerase Holoenzyme

1997 ◽  
Vol 272 (50) ◽  
pp. 31666-31676 ◽  
Author(s):  
Paola Pietroni ◽  
Mark C. Young ◽  
Gary J. Latham ◽  
Peter H. von Hippel
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Sliding Clamp

scholarly journals Structural Analyses of gp45 Sliding Clamp Interactions during Assembly of the Bacteriophage T4 DNA Polymerase Holoenzyme

1997 ◽  
Vol 272 (50) ◽  
pp. 31677-31684 ◽  
Author(s):  
Gary J. Latham ◽  
Daniel J. Bacheller ◽  
Paola Pietroni ◽  
Peter H. von Hippel
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Sliding Clamp

scholarly journals The SOS Error-Prone DNA Polymerase V Mutasome and β-Sliding Clamp Acting in Concert on Undamaged DNA and during Translesion Synthesis

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1083
Author(s):  
Adhirath Sikand ◽  
Malgorzata Jaszczur ◽  
Linda B. Bloom ◽  
Roger Woodgate ◽  
Michael M. Cox ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Pathogenic Bacteria ◽  
Fold Increase ◽  
Translesion Dna Synthesis ◽  
Sliding Clamp ◽  
Pol V ◽  
Dna Polymerase V ◽  
Acting In Concert

In the mid 1970s, Miroslav Radman and Evelyn Witkin proposed that Escherichia coli must encode a specialized error-prone DNA polymerase (pol) to account for the 100-fold increase in mutations accompanying induction of the SOS regulon. By the late 1980s, genetic studies showed that SOS mutagenesis required the presence of two “UV mutagenesis” genes, umuC and umuD, along with recA. Guided by the genetics, decades of biochemical studies have defined the predicted error-prone DNA polymerase as an activated complex of these three gene products, assembled as a mutasome, pol V Mut = UmuD’2C-RecA-ATP. Here, we explore the role of the β-sliding processivity clamp on the efficiency of pol V Mut-catalyzed DNA synthesis on undamaged DNA and during translesion DNA synthesis (TLS). Primer elongation efficiencies and TLS were strongly enhanced in the presence of β. The results suggest that β may have two stabilizing roles: its canonical role in tethering the pol at a primer-3’-terminus, and a possible second role in inhibiting pol V Mut’s ATPase to reduce the rate of mutasome-DNA dissociation. The identification of umuC, umuD, and recA homologs in numerous strains of pathogenic bacteria and plasmids will ensure the long and productive continuation of the genetic and biochemical journey initiated by Radman and Witkin.

scholarly journals Genetic evidence for two protein domains and a potential new activity in bacteriophage T4 DNA polymerase.

Genetics ◽  
1990 ◽  
Vol 124 (2) ◽  
pp. 213-220 ◽  
Author(s):  
L J Reha-Krantz
Keyword(s):  
Dna Polymerase ◽  
Bacteriophage T4 ◽  
Rnase H ◽  
Ribonuclease H ◽  
Temperature Sensitive ◽  
Polymerase Gene ◽  
Dna Polymerase I ◽  
E Coli ◽  
Intragenic Complementation ◽  
Polymerase I

Abstract Intragenic complementation was detected within the bacteriophage T4 DNA polymerase gene. Complementation was observed between specific amino (N)-terminal, temperature-sensitive (ts) mutator mutants and more carboxy (C)-terminal mutants lacking DNA polymerase polymerizing functions. Protein sequences surrounding N-terminal mutation sites are similar to sequences found in Escherichia coli ribonuclease H (RNase H) and in the 5'----3' exonuclease domain of E. coli DNA polymerase I. These observations suggest that T4 DNA polymerase, like E. coli DNA polymerase I, contains a discrete N-terminal domain.

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