Altered Oligomerization Properties of N316 Mutants of Escherichia coli TyrR
Keyword(s):
ABSTRACT The transcriptional regulator TyrR is known to undergo a dimer-to-hexamer conformational change in response to aromatic amino acids, through which it controls gene expression. In this study, we identified N316D as the second-site suppressor of Escherichia coli TyrRE274Q, a mutant protein deficient in hexamer formation. N316 variants exhibited altered in vivo regulatory properties, and the most drastic changes were observed for TyrRN316D and TyrRN316R mutants. Gel filtration analyses revealed that the ligand-mediated oligomer formation was enhanced and diminished for TyrRN316D and TyrRN316R, respectively, compared with the wild-type TyrR. ADP was substituted for ATP in the oligomer formation of TyrRN316D.
Keyword(s):
2002 ◽
Vol 184
(12)
◽
pp. 3167-3175
◽
Keyword(s):
1999 ◽
Vol 181
(9)
◽
pp. 2759-2764
◽
1987 ◽
Vol 7
(1)
◽
pp. 294-304
◽
Keyword(s):
1984 ◽
Vol 62
(5)
◽
pp. 276-279
◽
Keyword(s):