The DNA-binding protein II from Zymomonas mobilis. Complete amino acid sequence and interaction with DNA.
The primary structure of the DNA-binding protein II from Zymomonas mobilis has been determined from data provided by automated Edman degradation of the intact protein and of peptides derived from cleavage at aspartic acid and arginine residues. When compared with the homologous protein isolated from other bacteria, the DNA-binding protein II from Z mobilis shows many substitutions. Several non-conservative substitutions at positions usually highly conserved in this type of protein probably account for the weaker DNA-binding activity of this protein compared to that of the E coli protein.
Laine
B
B
U459 INSERM, Laboratoire de Biochimie Structurale, Faculté de Médecine, Lille, France.
Chartier
F
F
Culard
F
F
Bélaïche
D
D
Sautière
P
P
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000378:metabolism; D017355:Zymomonas / Q000378:metabolism*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria; D001224:Aspartic Acid; D004247:DNA; C044499:submandibular proteinase A; D012697:Serine Endopeptidases