Archaeal RadA protein binds DNA as both helical filaments and octameric rings

Journal of Molecular Biology

Volumn 314, Issue 5, 2001, Pages 1077-1085

  Yang, Shixin ^a   Yu, Xiong ^a   Seitz, Erica M ^b   Kowalczykowski, Stephen C ^b   Egelman, Edward H ^a  

^a UNIVERSITY OF VIRGINIA HEALTH SYSTEM   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Electron microscopy; Image analysis; Protein DNA complexes; Recombination; Ring proteins

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; DNA BINDING PROTEIN; PROTEIN DMC1; RAD51 PROTEIN; RADA PROTEIN; RECA PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GENETIC ANALYSIS; IMAGE ANALYSIS; MEIOSIS; PHYLOGENY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; SULFOLOBUS SOLFATARICUS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; SULFOLOBUS; SULFOLOBUS SOLFATARICUS;

EID: 0035861994     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.5213     Document Type: Article

References (47)

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15. recA-like genes from three archaean species with putative protein products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae
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17. The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 degrees C
18. Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy
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