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Originally published In Press as doi:10.1074/jbc.M206249200 on September 26, 2002

J. Biol. Chem., Vol. 277, Issue 49, 46998-47003, December 6, 2002
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A Key Role for the alpha 1 Helix of Human RAP74 in the Initiation and Elongation of RNA Chains*

Janel D. FunkDagger , Yuri A. Nedialkov, Dianpeng Xu, and Zachary F. Burton§

From the Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824-1319

RNA polymerase II-associating protein 74 (RAP74) is the large subunit of transcription factor IIF (TFIIF), which is essential for accurate initiation and stimulates elongation by RNA polymerase II. Mutations within or adjacent to the alpha 1 helix of the RAP74 subunit have been shown to decrease both initiation and elongation stimulation activities without strongly affecting the interactions of RAP74 with the RAP30 subunit or the interaction between TFIIF and RNA polymerase II. In this manuscript, mutations within the alpha 1 helix are compared with mutations made throughout the neighboring conserved N-terminal domain of RAP74. Changes within the N-terminal domain include disruptions of specific contacts with the alpha 1 helix, which were revealed in the recently published x-ray crystal structure (Gaiser, F., Tan, S., and Richmond, T. J. (2000) J. Mol. Biol. 302, 1119-1127). Contacts between the beta 4-beta 5 loop and the alpha 1 helix are shown to be largely unimportant for alpha 1 helix function. Other mutations throughout the N-terminal domain are consistent with the establishment of the dimer interface with the RAP30 subunit. The RAP74-RAP30 interface is important for TFIIF function, but no particular RAP74 amino acids within this region have been identified that are required for TFIIF activities. The molecular target of the alpha 1 helix remains unknown, but our studies refocus attention on this important functional motif of TFIIF.

* This work was supported by a grant from the National Institutes of Health (to Z. F. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by the Hughes Undergraduate Research Program at Michigan State University.

§ To whom correspondence should be addressed. Tel.: 517-353-0859; Fax: 517-353-9334; E-mail: Burton@msu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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