Cloning and sequence analysis of a novel member of the single-stranded DNA binding protein family.
A single-stranded DNA binding protein (SSB) was isolated which has unusual amino acid residues at sites previously shown to be highly conserved and critical for DNA binding. Sequence analysis suggested that these residues are characteristic of a novel class of SSBs from Gram-positive bacteria.
Rikke
B A
BA
Department of Cellular and Structural Biology, University of Texas Health Science Center at San Antonio, 78284-7762.
Vellanoweth
R L
RL
Her
S
S
Chatterje
B
B
Roy
A K
AK
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics*; D005796:Genes; D006094:Gram-Positive Bacteria / Q000235:genetics; D008969:Molecular Sequence Data; D051381:Rats / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins