A Motif Shared by TFIIF and TFIIB Mediates Their Interaction with the RNA Polymerase II Carboxy-Terminal Domain Phosphatase Fcp1p in Saccharomyces cerevisiae

doi:10.1128/MCB.20.20.7438-7449.2000

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Molecular and Cellular Biology, October 2000, p. 7438-7449, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A Motif Shared by TFIIF and TFIIB Mediates Their Interaction with the RNA Polymerase II Carboxy-Terminal Domain Phosphatase Fcp1p in Saccharomyces cerevisiae

Michael S. Kobor,¹^,² Lisa D. Simon,¹ Jim Omichinski,¹^,³ Guoqing Zhong,¹ Jacques Archambault,⁴ and Jack Greenblatt¹^,²^,^*

Banting and Best Department of Medical Research¹ and Department of Molecular and Medical Genetics,² University of Toronto, Toronto, Ontario M5G 1L6, and Department of Biological Sciences, Boehringer Ingelheim (Canada) Limited, Laval, Quebec H7S 2G5,⁴ Canada, and Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602³

Received 13 June 2000/Returned for modification 16 July 2000/Accepted 31 July 2000

Transcription by RNA polymerase II is accompanied by cyclic phosphorylation and dephosphorylation of the carboxy-terminalheptapeptide repeat domain (CTD) of its largest subunit. We haveused deletion and point mutations in Fcp1p, a TFIIF-interactingCTD phosphatase, to show that the integrity of its BRCT domain,like that of its catalytic domain, is important for cell viability,mRNA synthesis, and CTD dephosphorylation in vivo. Although regionsof Fcp1p carboxy terminal to its BRCT domain and at its aminoterminus were not essential for viability, deletion of eitherof these regions affected the phosphorylation state of the CTD.Two portions of this carboxy-terminal region of Fcp1p bound directlyto the first cyclin-like repeat in the core domain of the generaltranscription factor TFIIB, as well as to the RAP74 subunit ofTFIIF. These regulatory interactions with Fcp1p involved closelyrelated amino acid sequence motifs in TFIIB and RAP74. Mutatingthe Fcp1p-binding motif KEFGK in the RAP74 (Tfg1p) subunit ofTFIIF to EEFGE led to both synthetic phenotypes in certain fcp1tfg1 double mutants and a reduced ability of Fcp1p to activatetranscription when it is artificially tethered to a promoter.These results suggest strongly that this KEFGK motif in RAP74mediates its interaction with Fcp1p invivo.

^* Corresponding author. Mailing address: Banting and Best Department of Medical Research, University of Toronto, 112 CollegeSt., Rm. 210, Toronto, Ontario, Canada M5G 1L6. Phone: (416) 978-4141.Fax: (416) 978-8528. E-mail: jack.greenblatt{at}utoronto.ca.

Molecular and Cellular Biology, October 2000, p. 7438-7449, Vol. 20, No. 20
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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