The carboxyl terminus of RAP30 is similar in sequence to region 4 of bacterial sigma factors and is required for function

• Published in: The Journal of biological chemistry Vol. 267; no. 33; pp. 23942 - 23949
• Main Authors: GARRRETT, K. P, SERIZAWA, H, HANLEY, J. P, BRADSHER, J. N, TSUBOI, A, ARAI, N, YOKOTA, T, ARAI, K.-I, CONAWAY, R. C, CONAWAY, J. W
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 25.11.1992
• Subjects: Amino Acid Sequence; Animals; Antibodies; Bacillus subtilis; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA - genetics; Fundamental and applied biological sciences. Psychology; Humans; Immunoblotting; Kinetics; Liver - physiology; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Peptides - chemical synthesis; Peptides - immunology; Rats; Recombinant Proteins - analysis; Recombinant Proteins - metabolism; Sequence Deletion; Sequence Homology, Amino Acid; Sigma Factor - analysis; Sigma Factor - genetics; Sigma Factor - metabolism; Transcription Factors - analysis; Transcription Factors - genetics; Transcription Factors - metabolism; Transcription Factors, TFII; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Vertebrata; Mammalia; C terminal peptide; Rat; Structure activity relation; Transcription; Rodentia; Initiation factor σ; Transcription factor; Aminoacid sequence
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)35928-3

Transcription factor beta gamma (RAP30/74) from rat liver was previously shown in biochemical studies to control the binding of RNA polymerase II to promoters by a mechanism analogous to that utilized by bacterial sigma factors, by decreasing the affinity of polymerase for nonpromoter sites on DNA and by increasing the affinity of the enzyme for the preinitiation complex (Conaway, R. C., Garrett, K. P., Hanley, J. P., and Conaway, J. W. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 6205-6209). By constructing and analyzing mutants of beta gamma, we have identified a novel functional domain located in the carboxyl terminus of the gamma (RAP30) subunit. This domain shares sequence similarity with region 4 of bacterial sigma factors; in particular, it exhibits striking similarity to the carboxyl-terminal regions 4.1 and 4.2 of SpoIIIC (Bacillus subtilis sigma k). Evidence from biochemical studies argues that a mutant gamma (RAP30), lacking amino acid sequences similar to sigma homology region 4.2, is able to assemble with the beta (RAP74) subunit to form a mutant beta gamma (RAP30/74) with impaired ability to interact with RNA polymerase II.