Isolation of DNA-Binding Membrane Proteins fromBacillus subtilis
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چکیده
منابع مشابه
ISOLATION AND PURIFICATION OF MAJOR OUTER MEMBRANE PROTEINS FROM BRUCELLA ABORTUS S-99
Isolation and purification of major outer membrane proteins (OMP) from the cell wall envelope of Brucella abortus S-99 were achieved by sonication, solubilization and membrane fractionation in the presence of non-ionic detergent (Tx-100) and lysozyme treatments, followed by ultracentrifugation. The crude OMP was treated with trypsin to free the preparation from any other protein contaminan...
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Microorganisms use a number of small basic proteins for organization and compaction of their DNA. By their interaction with the genome, these proteins do have a profound effect on gene expression, growth behavior, and viability. It has to be distinguished between indirect effects as a consequence of the state of chromosome condensation and relaxation that influence the rate of RNA polymerase ac...
متن کاملGenetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins
We have investigated the structural, biochemical and cellular roles of the two single-stranded (ss) DNA-binding proteins from Bacillus subtilis, SsbA and SsbB. During transformation, SsbB localizes at the DNA entry pole where it binds and protects internalized ssDNA. The 2.8-Å resolution structure of SsbB bound to ssDNA reveals a similar overall protein architecture and ssDNA-binding surface to...
متن کاملIsolation of Ku70-binding proteins (KUBs).
DNA-dependent protein kinase (DNA-PK) plays a critical role in resealing DNA double-stand breaks by non-homologous end joining. Aside from DNA-PK, XRCC4 and DNA ligase IV, other proteins which play a role(s) in this repair pathway remain unknown; DNA-PK contains a catalytic subunit (DNA-PKcs) and a DNA binding subunit (Ku70 and Ku80). We isolated Ku70-binding proteins (KUB1-KUB4) using yeast tw...
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ژورنال
عنوان ژورنال: Microbiology and Immunology
سال: 1983
ISSN: 0385-5600
DOI: 10.1111/j.1348-0421.1983.tb00607.x