NDLI: Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37.

Content Provider	Journal of Biological Chemistry (JBC)
Author	Christie, K. R. Awrey, D. E. Edwards, A. M. Kane, C. M.
Abstract	Saccharomyces cerevisiae has a TFIIS-related transcription elongation factor, originally called P37 (Sawadogo, M., Sentenac, A., and Fromageot, P. (1979) J. Biol. Chem. 255, 12-15; Nakanishi, T., Nakano, A., Nomura, K., Sekimizu, K., and Natori, S. (1992) J. Biol. Chem. 267, 13200-13204), which binds directly to RNA polymerase II and stimulates read-through of intrinsic blocks to elongation. To elucidate functional features of this protein:protein interaction, we tested the ability of several forms of RNA polymerase II to respond to either full-length or an amino-terminal truncation of TFIIS. The variants of the polymerase differed in the structure of the carboxyl-terminal domain of the largest subunit or lacked two of the smaller subunits. No differences in ability to recognize intrinsic blocks to elongation or to read through them in response to either form of TFIIS were detected among these variants. Furthermore, ternary complexes containing each variant form of RNA polymerase cleave the 3' end of the nascent transcripts in response to TFIIS, a reaction previously reported for mammalian and Drosophila TFIIS (Kassavetis, G. A., and Geiduschek, E. P. (1993) Science 259, 944-945) and likely to be important in TFIIS function. Thus the carboxyl-terminal domain of the largest subunit and subunits four and seven of the polymerase, required in vivo, are not required in vitro for recognition of intrinsic blocks to elongation, read-through in response to TFIIS, or TFIIS-stimulated cleavage of the nascent transcript.
Related Links	http://www.jbc.org/content/269/2/936.abstract
Ending Page	943
Starting Page	936
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	2
Volume Number	269
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1994-01-14
Access Restriction	Open
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Yeast Transcript Elongation Factor (TFIIS), Structure and Function II: RNA POLYMERASE BINDING, TRANSCRIPT CLEAVAGE, AND READ-THROUGH

Cleavage of the nascent transcript induced by TFIIS is insufficient to promote read-through of intrinsic blocks to elongation by RNA polymerase II.

Transcription elongation factor SII (TFIIS) enables RNA polymerase II to elongate through a block to transcription in a human gene in vitro.

Intrinsic Transcript Cleavage in Yeast RNA Polymerase II Elongation Complexes

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Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II.

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Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37.

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