hMSH2–hMSH6 Forms a Hydrolysis-Independent Sliding Clamp on Mismatched DNA
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چکیده
منابع مشابه
Structure of a Sliding Clamp on DNA
The structure of the E. coli beta clamp polymerase processivity factor has been solved in complex with primed DNA. Interestingly, the clamp directly binds the DNA duplex and also forms a crystal contact with the ssDNA template strand, which binds into the protein-binding pocket of the clamp. We demonstrate that these clamp-DNA interactions function in clamp loading, perhaps by inducing the ring...
متن کاملDivision of labor--sequential ATP hydrolysis drives assembly of a DNA polymerase sliding clamp around DNA.
The beta sliding clamp encircles DNA and enables processive replication of the Escherichia coli genome by DNA polymerase III holoenzyme. The clamp loader, gamma complex, assembles beta around DNA in an ATP-fueled reaction. Previous studies have shown that gamma complex opens the beta ring and also interacts with DNA on binding ATP. Here, a rapid kinetic analysis demonstrates that gamma complex ...
متن کاملHow a DNA polymerase clamp loader opens a sliding clamp.
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 DNA. The clamp loader traps a spiral conformation of the ope...
متن کاملLoading Dynamics of a Sliding DNA Clamp**
Sliding DNA clamps are loaded at a ss/dsDNA junction by a clamp loader that depends on ATP binding for clamp opening. Sequential ATP hydrolysis results in closure of the clamp so that it completely encircles and diffuses on dsDNA. We followed events during loading of an E. coli β clamp in real time by using single-molecule FRET (smFRET). Three successive FRET states were retained for 0.3 s, 0.7...
متن کاملThe sliding clamp of DNA polymerase III holoenzyme encircles DNA.
DNA polymerases that duplicate chromosomes are remarkably processive multiprotein machines. These replicative polymerases remain in continuous association with the DNA over tens to hundreds of kilobases. What is the chemical basis of their strong grip to the template? The mystery behind the high processivity of the replicative polymerase of the Escherichia coli chromosome, DNA polymerase III ho...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 1999
ISSN: 1097-2765
DOI: 10.1016/s1097-2765(00)80316-0