Domain structure of the large subunit of Escherichia coli carbamoyl phosphate synthetase. Location of the binding site for the allosteric inhibitor UMP in the carboxy-terminal domain

Biochemistry ◽  
1991 ◽  
Vol 30 (4) ◽  
pp. 1068-1075 ◽  
Author(s):  
Vicente Rubio ◽  
Javier Cervera ◽  
Carol J. Lusty ◽  
Elena Bendala ◽  
Hubert G. Britton
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Domain Structure ◽  
Large Subunit ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Allosteric Inhibitor ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal

scholarly journals Expression of the Bordetella pertussis P.69 pertactin adhesin in Escherichia coli: fate of the carboxy-terminal domain

Microbiology ◽  
1994 ◽  
Vol 140 (12) ◽  
pp. 3301-3308 ◽  
Author(s):  
I. Charles ◽  
N. Fairweather ◽  
D. Pickard ◽  
J. Beesley ◽  
R. Anderson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bordetella Pertussis ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal

scholarly journals Analysis of the role of TFIIE in basal transcription and TFIIH-mediated carboxy-terminal domain phosphorylation through structure-function studies of TFIIE-alpha.

1995 ◽  
Vol 15 (9) ◽  
pp. 4856-4866 ◽  
Author(s):  
Y Ohkuma ◽  
S Hashimoto ◽  
C K Wang ◽  
M Horikoshi ◽  
R G Roeder
Keyword(s):  
Rna Polymerase Ii ◽  
Transcription Initiation ◽  
Large Subunit ◽  
Strong Interactions ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
C Terminus ◽  
Transcription Initiation Complex ◽  
Carboxy Terminal ◽  
Ctd Phosphorylation

The general transcription factor TFIIE recruits TFIIH at a late stage of transcription initiation complex formation and markedly stimulates TFIIH-dependent phosphorylation of the carboxy-terminal domain (CTD) of RNA polymerase II. To study this function of TFIIE in more detail, systematic deletion mutations were introduced into the large subunit of TFIIE (TFIIE-alpha) and were analyzed with regard to their effects on TFIIH-dependent CTD phosphorylation, TFIIE-dependent basal and enhancer-dependent transcription, and interactions of TFIIE-alpha with both TFIIE-beta and TFIIH. The amino (N)-terminal half of TFIIE-alpha, which possesses several putative structural motifs, was sufficient for the phosphorylation and transcription activities and for TFIIE-beta interactions, whereas a site effecting both strong interactions with TFIIH and large stimulatory effects on transcription and CTD phosphorylation was localized to an acidic region near the carboxy (C) terminus. The fact that these activities appear to be tightly linked supports the idea that TFIIE interacts physically and functionally with TFIIH and that CTD phosphorylation is essential for transcription under normal conditions. The present results suggest that TFIIE, via its effect on TFIIH, may act as a checkpoint for formation of a preinitiation complex.

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