scholarly journals Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex

2006 ◽  
Vol 103 (31) ◽  
pp. 11544-11548 ◽  
Author(s):  
Y.-W. Han ◽  
T. Tani ◽  
M. Hayashi ◽  
T. Hishida ◽  
H. Iwasaki ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Direct Observation ◽  
Protein Complex ◽  
Holliday Junction ◽  
Branch Migration

scholarly journals 2P097 Direct observation of the RuvA-RuvB mediated branch migration of Holliday junction DNA with single-molecule analysis

2004 ◽  
Vol 44 (supplement) ◽  
pp. S134
Author(s):  
Y.-W. Han ◽  
T. Tani ◽  
M. Hayashi ◽  
T. Hishida ◽  
H. Iwasaki ◽  
...  
Keyword(s):  
Direct Observation ◽  
Single Molecule ◽  
Holliday Junction ◽  
Branch Migration ◽  
Single Molecule Analysis

scholarly journals Polarity and Bypass of DNA Heterology during Branch Migration of Holliday Junctions by Human RAD54, BLM, and RECQ1 Proteins

2012 ◽  
Vol 287 (15) ◽  
pp. 11820-11832 ◽  
Author(s):  
Olga M. Mazina ◽  
Matthew J. Rossi ◽  
Julianna S. Deakyne ◽  
Fei Huang ◽  
Alexander V. Mazin
Keyword(s):  
Escherichia Coli ◽  
Dna Repair ◽  
Holliday Junctions ◽  
Holliday Junction ◽  
Helicase Activity ◽  
Branch Migration ◽  
Blm Helicase ◽  
Human Rad51

Several proteins have been shown to catalyze branch migration (BM) of the Holliday junction, a key intermediate in DNA repair and recombination. Here, using joint molecules made by human RAD51 or Escherichia coli RecA, we find that the polarity of the displaced ssDNA strand of the joint molecules defines the polarity of BM of RAD54, BLM, RECQ1, and RuvAB. Our results demonstrate that RAD54, BLM, and RECQ1 promote BM preferentially in the 3′→5′ direction, whereas RuvAB drives it in the 5′→3′ direction relative to the displaced ssDNA strand. Our data indicate that the helicase activity of BM proteins does not play a role in the heterology bypass. Thus, RAD54 that lacks helicase activity is more efficient in DNA heterology bypass than BLM or REQ1 helicases. Furthermore, we demonstrate that the BLM helicase and BM activities require different protein stoichiometries, indicating that different complexes, monomers and multimers, respectively, are responsible for these two activities. These results define BM as a mechanistically distinct activity of DNA translocating proteins, which may serve an important function in DNA repair and recombination.

scholarly journals The dnaB-dnaC replication protein complex of Escherichia coli

1989 ◽  
Vol 264 (5) ◽  
pp. 2463-2468 ◽  
Author(s):  
E Wahle ◽  
R S Lasken ◽  
A Kornberg
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Replication Protein

scholarly journals The dnaB-dnaC replication protein complex of Escherichia coli

1989 ◽  
Vol 264 (5) ◽  
pp. 2469-2475
Author(s):  
E Wahle ◽  
R S Lasken ◽  
A Kornberg
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Replication Protein

Crystallization of E. coli RuvA gives insights into the symmetry of a Holliday junction/protein complex

1997 ◽  
Vol 53 (1) ◽  
pp. 122-124 ◽  
Author(s):  
S. E. Sedelnikova ◽  
J. B. Rafferty ◽  
D. Hargreaves ◽  
A. A. Mahdi ◽  
R. G. Lloyd ◽  
...  
Keyword(s):  
Protein Complex ◽  
Holliday Junction ◽  
E Coli ◽  
Junction Protein

scholarly journals Reductive alkylation of ribosomes as a probe to the topography of ribosomal proteins*

1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Reductive Alkylation ◽  
Lysine Residues

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.

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