A partially functional 245-amino-acid internal deletion derivative of Escherichia coli sigma 70.
AUTOR(ES)
Kumar, A
RESUMO
Two hundred forty-five consecutive amino acids of the sigma 70 subunit of Escherichia coli RNA polymerase are not conserved in the homologous protein of Bacillus subtilis. We show that their deletion from a sigma 70-32 hybrid protein caused no severe loss of function in vivo, while sigma 70 itself retained considerable function in vitro.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=177307Documentos Relacionados
- Dominant lethal phenotype of a mutation in the -35 recognition region of Escherichia coli sigma 70.
- Influence of a glycine or proline substitution on the functional properties of a 14-amino-acid analog of Escherichia coli heat-stable enterotoxin.
- Citrobacter freundii produces an 18-amino-acid heat-stable enterotoxin identical to the 18-amino-acid Escherichia coli heat-stable enterotoxin (ST Ia).
- Functional complementation of internal deletion mutants in the lactose permease of Escherichia coli.
- A Carboxy-Terminal 16-Amino-Acid Region of ς38 of Escherichia coli Is Important for Transcription under High-Salt Conditions and Sigma Activities In Vivo