TY - JOUR
T1 - Identification of a subunit assembly domain in the alpha subunit of Escherichia coli RNA polymerase
AU - Igarashi, Kazuhiko
AU - Fujita, Nobuyuki
AU - Ishihama, Akira
N1 - Funding Information:
Wti thank Drs S. Mat,suyama and S. Mizushima ([Tniversitg of Tokyo) for a generous gift of plasmids, Dr K. Nagat,a (IVIG) for valua.btr suggestions, and I)r R. 8. Hayward (Universit’y of Edinburgh) for critical reading of the manuscript. This work was supported by (irants-in-Aid from the Ministry of Education, Science and Culture of ,Japan.
PY - 1991/3/5
Y1 - 1991/3/5
N2 - The α subunit of Escherichia coli DNA-dependent RNA polymerase is encoded by the rpoA gene and plays a major role in enzyme assembly. A set of C-terminal deletion mutations of the rpoA gene was constructed. The results of mixed reconstitution experiments in vitro, using the truncated α polypeptides encoded by the rpoA deletion mutants, suggest that the amino-terminal two-thirds of α subunit is sufficient for the formation of pseudo-core complexes containing both β and β′ subunits.
AB - The α subunit of Escherichia coli DNA-dependent RNA polymerase is encoded by the rpoA gene and plays a major role in enzyme assembly. A set of C-terminal deletion mutations of the rpoA gene was constructed. The results of mixed reconstitution experiments in vitro, using the truncated α polypeptides encoded by the rpoA deletion mutants, suggest that the amino-terminal two-thirds of α subunit is sufficient for the formation of pseudo-core complexes containing both β and β′ subunits.
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U2 - 10.1016/0022-2836(91)90865-4
DO - 10.1016/0022-2836(91)90865-4
M3 - Article
C2 - 2002495
AN - SCOPUS:0026019420
SN - 0022-2836
VL - 218
SP - 1
EP - 6
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -