Variability in the nucleic acid binding site size and the amount of single-stranded DNA-binding protein inEscherichia coli

FEBS Letters ◽  
1985 ◽  
Vol 181 (1) ◽  
pp. 133-137 ◽  
Author(s):  
E.V. Bobst ◽  
A.M. Bobst ◽  
F.W. Perrino ◽  
R.R. Meyer ◽  
D.C. Rein
Keyword(s):  
Nucleic Acid ◽  
Dna Binding ◽  
Binding Site ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Inescherichia Coli ◽  
Nucleic Acid Binding ◽  
Single Stranded Dna

scholarly journals CC1, a Novel Crenarchaeal DNA Binding Protein

2006 ◽  
Vol 189 (2) ◽  
pp. 403-409 ◽  
Author(s):  
Xiao Luo ◽  
Uli Schwarz-Linek ◽  
Catherine H. Botting ◽  
Reinhard Hensel ◽  
Bettina Siebers ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Nucleic Acid Binding ◽  
Chromatin Protein ◽  
Gene Encoding ◽  
Single Stranded Dna ◽  
Cell Extracts ◽  
Domains Of Life ◽  
High Level

ABSTRACT The genomes of the related crenarchaea Pyrobaculum aerophilum and Thermoproteus tenax lack any obvious gene encoding a single-stranded DNA binding protein (SSB). SSBs are essential for DNA replication, recombination, and repair and are found in all other genomes across the three domains of life. These two archaeal genomes also have only one identifiable gene encoding a chromatin protein (the Alba protein), while most other archaea have at least two different abundant chromatin proteins. We performed a biochemical screen for novel nucleic acid binding proteins present in cell extracts of T. tenax. An assay for proteins capable of binding to a single-stranded DNA oligonucleotide resulted in identification of three proteins. The first protein, Alba, has been shown previously to bind single-stranded DNA as well as duplex DNA. The two other proteins, which we designated CC1 (for crenarchaeal chromatin protein 1), are very closely related to one another, and homologs are restricted to the P. aerophilum and Aeropyrum pernix genomes. CC1 is a 6-kDa, monomeric, basic protein that is expressed at a high level in T. tenax. This protein binds single- and double-stranded DNAs with similar affinities. These properties are consistent with a role for CC1 as a crenarchaeal chromatin protein.

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