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

J. Biol. Chem., Vol. 277, Issue 37, 33580-33589, September 13, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/37/33580    most recent M205415200v1 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 Kozak, L. Articles by Dhar, R. Search for Related Content PubMed PubMed Citation Articles by Kozak, L. Articles by Dhar, R. Social Bookmarking                      What's this?

Elf1p, a Member of the ABC Class of ATPases, Functions as a mRNA Export Factor in Schizosacchromyces pombe^*

Libor Kozak, Ganesh Gopal, Jin Ho Yoon^§, Zuben E. Sauna^¶, Suresh V. Ambudkar^¶, Anjan G. Thakurta, and Ravi Dhar

From the  Basic Research Laboratory and ^¶ Laboratory of Cell Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892

Rae1p and Mex67p/Tap are conserved mRNA export factors. We have used synthetic lethal genetic screens in Schizosaccharomyces pombe to identify mutations in genes that are functionally linked to rae1 and mex67 in mRNA export. From these screens, we have isolated mutations in a putative S. pombe homologue of the Candida albicans elf1 gene. The elf1 of S. pombe is not an essential gene. When elf1 mutations are combined with rae1-167 mutation, growth and mRNA export is inhibited in the double mutants. This inhibition can be suppressed by the multicopy expression of mex67 suggesting that Mex67p can substitute for the loss of Elf1p function. Elf1p is a non-membrane member of the ATP-binding cassette (ABC) class of ATPase and the GFP-Elf1p fusion localizes to the cytoplasm. Elf1p, expressed and purified from Escherichia coli, binds and hydrolyzes ATP. A mutant Elf1p that carries a glycine to aspartic acid (G731D) mutation within the Walker A domain of the second ATP site retains the ATP binding but loses its ATPase activity in vitro. This mutant protein no longer functions in mRNA export. Taken together, our results show that Elf1p functions as a mRNA export factor along with Rae1p and Mex67p in S. pombe.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. A. Burke, R. K. Mutharasan, and H. Ardehali The Sulfonylurea Receptor, an Atypical ATP-Binding Cassette Protein, and Its Regulation of the KATP Channel Circ. Res., February 1, 2008; 102(2): 164 - 176. [Abstract] [Full Text] [PDF]

				A. G. Thakurta, S. P. Selvanathan, A. D. Patterson, G. Gopal, and R. Dhar The Nuclear Export Signal of Splicing Factor Uap56p Interacts with Nuclear Pore-associated Protein Rae1p for mRNA Export in Schizosaccharomyces pombe J. Biol. Chem., June 15, 2007; 282(24): 17507 - 17516. [Abstract] [Full Text] [PDF]

				K. J. Linton Structure and Function of ABC Transporters Physiology, April 1, 2007; 22(2): 122 - 130. [Abstract] [Full Text] [PDF]

				Z. E. Sauna, K. Nandigama, and S. V. Ambudkar Exploiting Reaction Intermediates of the ATPase Reaction to Elucidate the Mechanism of Transport by P-glycoprotein (ABCB1) J. Biol. Chem., September 8, 2006; 281(36): 26501 - 26511. [Abstract] [Full Text] [PDF]