Comparison of the Assembly of the Bacteriophage T4 Clamp
AbstractProper formation of the bacteriophage T4 DNA polymerase holoenzyme requires a wide spectrum of protein–protein and protein–DNA interactions among the DNA polymerase gp43, the sliding clamp gp45, and gp44/62, the clamp loader complex (CLC). The 44 and 62 proteins associate to form a tight complex maintained in a 4:1 ratio.
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Creating a dynamic picture of the sliding clamp during T4
Jul 17, 2001 · The coordinated assembly of the DNA polymerase (gp43), the sliding clamp (gp45), and the clamp loader (gp44/62) to form the bacteriophage T4 DNA polymerase holoenzyme is a multistep process. A partially opened toroid-shaped gp45 is loaded around DNA by gp44/62 in an ATP-dependent manner.
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In Vitro Reconstitution of the Bacteriophage T4 Clamp
The clamp loader complex (CLC) of bacteriophage T4 is essential for viability and has analogs in both prokaryotes and eukaryotes. The gp44 and gp62 subunits of …
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Selective inhibition of DNA replicase assembly by a non
Feb 19, 2010 · Clamp loaders across all species serve identical functions by using ATP to assemble their respective DNA replicase complexes . In fact, the clamp loaders from bacteriophage T4, E. coli, and eukaryotes all display significant similarity (~56%) and identity (~33%) in regions that interact with ATP (Supplemental Information 2). The similarities in
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How a DNA Polymerase Clamp Loader Opens a Sliding Clamp
Dec 23, 2011 · Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template …
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Clamp loaders and sliding clamps - ScienceDirect
Apr 01, 2002 · The bacteriophage T4 clamp loader is also constituted of five subunits (four copies of the gp44 ATPase and one copy of gp62) 42., 43.. In eukaryotes, the clamp loader is known as RFC (replication factor C) and is composed of five distinct proteins (RFCs 1–5) .
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Background: The high speed and processivity of replicative DNA polymerases reside in a processivity factor which has been shown to be a ring‐shaped protein. This protein ('sli
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RCSB PDB - 3U61: Structure of T4 Bacteriophage Clamp
Oct 11, 2011 · Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template …
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Cell, Vol. 106, 655–660, September 21, 2001, Copyright
that of, the first clamp loader subunit whose structure was determined (Guenther et al., 1997). Previous se-quence analyses of the eukaryotic clamp loader RFC revealed not only significant similarity with subunits of the prokaryotic clamp loader ( and for E. coli,T4 phage gp44), but also with a large number of proteins
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Comparison of the Assembly of the Bacteriophage T4 …
Jul 20, 1999 · Proper formation of the bacteriophage T4 DNA polymerase holoenzyme requires a wide spectrum of protein–protein and protein–DNA interactions among the DNA polymerase gp43, the sliding clamp gp45, and gp44/62, the clamp loader complex (CLC). The 44 and 62 proteins associate to form a tight complex maintained in a 4:1 ratio.
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The kinetic mechanism of formation of the bacteriophage T4
Structural analysis of bacteriophage T4 DNA replication: a
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Comparison of the assembly of the bacteriophage T4 …
Aug 01, 1999 · Comparison of the assembly of the bacteriophage T4 clamp loader complex (gp44/62) expressed in a cis versus trans genomic configuration. (PMID:10405357) PMID:10405357
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Creating a dynamic picture of the sliding clamp during T4
Jul 17, 2001 · The coordinated assembly of the DNA polymerase (gp43), the sliding clamp (gp45), and the clamp loader (gp44/62) to form the bacteriophage T4 DNA polymerase holoenzyme is a multistep process. A partially opened toroid-shaped gp45 is loaded around DNA by gp44/62 in an ATP-dependent manner. Gp43 binds to this complex to generate the holoenzyme in which …
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How a DNA Polymerase Clamp Loader Opens a Sliding Clamp
Organization of the T4 clamp loader complex. We crystallized the T4 bacteriophage clamp loader bound to an ATP analog, primer-template DNA and the sliding clamp. The T4 replicase has served as a key model system in studies of DNA replication (1, 23), but the T4 clamp loader had not been characterized structurally. We determined structures from
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Tracking Sliding Clamp Opening and Closing during
Feb 25, 2000 · The bacteriophage T4 DNA polymerase holoenzyme, consisting of the DNA polymerase (gp43), the sliding clamp (gp45), and the clamp loader (gp44/62), is loaded onto DNA in an ATP-dependent, multistep reaction. The trimeric, ring-shaped gp45 is loaded onto DNA such that the DNA passes through the center of the ring. gp43 binds to this complex, thereby …
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Clamp loaders and sliding clamps David Jeruzalmi, Mike O
The bacteriophage T4 clamp loader is also constituted of five subunits (four copies of the gp44 ATPase and one copy of gp62) [42,43]. In eukaryotes, the clamp loader is known as RFC (replication factor C) and is composed of five distinct proteins (RFCs 1–5) [44]. In archaebacteria, the clamp loader is formed from two kinds of subunits, large
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Comparison of the Assembly of the Bacteriophage T4 …
Structural analysis of bacteriophage T4 DNA replication: a
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