Open Access. Powered by Scholars. Published by Universities.®

Biochemistry, Biophysics, and Structural Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

2011

Series

DNA Repair

Articles 1 - 3 of 3

Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

An Interaction Between The Walker A And D-Loop Motifs Is Critical To Atp Hydrolysis And Cooperativity In Bacteriophage T4 Rad50, Metzere Bierlein De La Rosa, Scott W. Nelson Jul 2011

An Interaction Between The Walker A And D-Loop Motifs Is Critical To Atp Hydrolysis And Cooperativity In Bacteriophage T4 Rad50, Metzere Bierlein De La Rosa, Scott W. Nelson

Biochemistry, Biophysics and Molecular Biology Publications

The ATP binding cassette (ABC) proteins make up a large superfamily with members coming from all kingdoms. The functional form of the ABC protein nucleotide binding domain (NBD) is dimeric with ATP binding sites shared between subunits. The NBD is defined by six motifs: the Walker A, Q-loop, Signature, Walker-B, D-loop, and H-loop. The D-loop contains a conserved aspartate whose function is not clear but has been proposed to be involved in cross-talk between ATP binding sites. Structures of various ABC proteins suggest an interaction between the D-loop aspartate and an asparagine residue located in Walker A loop of the ...


Functional Evaluation Of Bacteriophage T4 Rad50 Signature Motif Residues, Timothy J. Herdendorf, Scott W. Nelson Jun 2011

Functional Evaluation Of Bacteriophage T4 Rad50 Signature Motif Residues, Timothy J. Herdendorf, Scott W. Nelson

Biochemistry, Biophysics and Molecular Biology Publications

The repair of DNA double-strand breaks (DSBs) is essential to maintaining the integrity of the genome, and organisms have evolved a conserved mechanism to facilitate their repair. In eukaryotes, archaea, and some bacteriophage, a complex made up of Mre11 and Rad50 (MR complex), which are a nuclease and ATPase, respectively, is involved in the initial processing of DSBs. Rad50 is a member of the ATP Binding Cassette (ABC) protein superfamily, the members of which contain an important Signature motif that acts in trans to complete the dimeric ATP binding site. To explore the functional relevance of this motif, four of ...


Biochemical Characterization Of Bacteriophage T4 Mre11-Rad50 Complex, Timothy J. Herdendorf, Dustin William Albrecht, Stephen J. Benkovic, Scott W, Nelson Jan 2011

Biochemical Characterization Of Bacteriophage T4 Mre11-Rad50 Complex, Timothy J. Herdendorf, Dustin William Albrecht, Stephen J. Benkovic, Scott W, Nelson

Biochemistry, Biophysics and Molecular Biology Publications

The Mre11-Rad50 complex (MR) from bacteriophage T4 (gp46/47) is involved in the processing of DNA double-strand breaks. Here, we describe the activities of the T4 MR complex and its modulation by proteins involved in homologous recombination. T4 Mre11 is a Rad50- and Mn2+-dependent dsDNA exonuclease and ssDNA endonuclease. ATP hydrolysis is required for the removal of multiple nucleotides via dsDNA exonuclease activity but not for the removal of the first nucleotide or for ssDNA endonuclease activity, indicating ATP hydrolysis is only required for repetitive nucleotide removal. By itself, Rad50 is a relatively inefficient ATPase, but the presence ...