HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 10, 8580-8585, March 7, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/10/8580    most recent M211384200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ubukata, T. Articles by Nakanishi, T. Search for Related Content PubMed PubMed Citation Articles by Ubukata, T. Articles by Nakanishi, T. Social Bookmarking                      What's this?

Cleavage, but Not Read-through, Stimulation Activity Is Responsible for Three Biologic Functions of Transcription Elongation Factor S-II^*

Toshiharu Ubukata, Tomoko Shimizu, Nobuaki Adachi, Kazuhisa Sekimizu^§, and Toshiyuki Nakanishi^¶

From the  Frontier Project 3, Proteome Research Laboratory, Daiichi Pharmaceutical Company, Ltd., 519 Shimo-Ishibashi, Ishibashi-machi, Shimotsuga-gun, Tochigi 329-0512, Japan and ^§ Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Transcription elongation factor S-II stimulates cleavage of nascent transcripts generated by RNA polymerase II stalled at transcription arrest sites. In vitro experiments have shown that this action promotes RNA polymerase II to read through these transcription arrest sites. This S-II-mediated cleavage is thought to be necessary, but not sufficient, to promote read-through in the in vitro systems. Therefore, Saccharomyces cerevisiae strains expressing S-II mutant proteins with different in vitro activities were used to study both the cleavage and the read-through stimulation activities of S-II to determine which S-II functions are responsible for its biologic functions. Strains expressing mutant S-II proteins active in both cleavage and read-through stimulation were as resistant as wild type strains to 6-azauracil and mycophenolic acid. 6-Azauracil also induced IMD2 gene expression in both these mutant strains and the wild type. Furthermore, strains having a genotype consisting of one of these S-II mutations and the spt4 null mutation grew as well as the spt4 null mutant at 37 °C, a restrictive temperature for a strain bearing double null mutations of spt4 and S-II. In contrast, strains bearing S-II mutations defective in both cleavage and read-through stimulation had phenotypes similar to those of an S-II null mutant. However, one strain expressing a mutant S-II protein active only in cleavage stimulation had a phenotype similar to that of the wild type strain. These results suggest that cleavage, but not read-through, stimulation activity is responsible for all three biologic functions of S-II (i.e. suppression of 6-azauracil sensitivity, induction of the IMD2 gene, and suppression of temperature sensitivity of spt4 null mutant).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Y. Ghavi-Helm, M. Michaut, J. Acker, J.-C. Aude, P. Thuriaux, M. Werner, and J. Soutourina Genome-wide location analysis reveals a role of TFIIS in RNA polymerase III transcription Genes & Dev., July 15, 2008; 22(14): 1934 - 1947. [Abstract] [Full Text] [PDF]

				B. Guglielmi, J. Soutourina, C. Esnault, and M. Werner TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo PNAS, October 9, 2007; 104(41): 16062 - 16067. [Abstract] [Full Text] [PDF]

				L. Rowen, E. Williams, G. Glusman, E. Linardopoulou, C. Friedman, M. E. Ahearn, J. Seto, C. Boysen, S. Qin, K. Wang, et al. Interchromosomal Segmental Duplications Explain the Unusual Structure of PRSS3, the Gene for an Inhibitor-Resistant Trypsinogen Mol. Biol. Evol., August 1, 2005; 22(8): 1712 - 1720. [Abstract] [Full Text] [PDF]

				C. Zhang, H. Yan, and Z. F. Burton Combinatorial Control of Human RNA Polymerase II (RNAP II) Pausing and Transcript Cleavage by Transcription Factor IIF, Hepatitis {delta} Antigen, and Stimulatory Factor II J. Biol. Chem., December 12, 2003; 278(50): 50101 - 50111. [Abstract] [Full Text] [PDF]

				W. Walter, M. L. Kireeva, V. M. Studitsky, and M. Kashlev Bacterial Polymerase and Yeast Polymerase II Use Similar Mechanisms for Transcription through Nucleosomes J. Biol. Chem., September 19, 2003; 278(38): 36148 - 36156. [Abstract] [Full Text] [PDF]