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Molecular and Cellular Biology, December 1998, p. 7139-7146, Vol. 18, No. 12
Department of Biology, Massachusetts
Institute of Technology, Cambridge, Massachusetts 02139
Received 15 May 1998/Returned for modification 26 June
1998/Accepted 28 August 1998
Secretory proteins in eukaryotic cells are transported to the cell
surface via the endoplasmic reticulum (ER) and the Golgi apparatus by
membrane-bounded vesicles. We screened a collection of
temperature-sensitive mutants of Saccharomyces cerevisiae
for defects in ER-to-Golgi transport. Two of the genes identified in
this screen were PRP2, which encodes a known pre-mRNA
splicing factor, and RSE1, a novel gene that we show to be
important for pre-mRNA splicing. Both prp2-13 and
rse1-1 mutants accumulate the ER forms of invertase and the
vacuolar protease CPY at restrictive temperature. The secretion defect
in each mutant can be suppressed by increasing the amount of
SAR1, which encodes a small GTPase essential for COPII
vesicle formation from the ER, or by deleting the intron from the
SAR1 gene. These data indicate that a failure to splice
SAR1 pre-mRNA is the specific cause of the secretion defects in prp2-13 and rse1-1. Moreover, these
data imply that Sar1p is a limiting component of the ER-to-Golgi
transport machinery and suggest a way that secretory pathway function
might be coordinated with the amount of gene expression in a cell.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Link between Secretion and Pre-mRNA Processing
Defects in Saccharomyces cerevisiae and the Identification
of a Novel Splicing Gene, RSE1
*
Corresponding author. Mailing address: Department of
Biology, Room 68-533, 77 Massachusetts Ave., Cambridge, MA 02139. Phone: (617) 253-9804. Fax: (617) 253-8699. E-mail:
ckaiser{at}mit.edu.
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