Genetics. Published Articles Ahead of Print: February 16, 2005, Copyright © 2005
doi:10.1534/genetics.104.034322


A more recent version of this article appeared on May 1, 2005.


REGULAR RESEARCH PAPERS

Mutations in the Saccharomyces cerevisae LSM1 gene that affect mRNA decapping and 3' end protection

1 Uniformed Services University of the Health Sciences (USUHS)
2 The University of Arizona

* To whom correspondence should be addressed. E-mail: tsundaresan{at}usuhs.mil.

Submitted on August 6, 2004
Revised on October 17, 2004
Accepted on 18 January 2005


Abstract

The decapping of eukaryotic mRNAs is a key step in their degradation. The heteroheptameric Lsm1p-7p complex is a general activator of decapping and also functions in protecting the 3' ends of deadenylated mRNAs from a 3' trimming reaction. Lsm1p is the unique member of the Lsm1p-7p complex distinguishing that complex from the functionally different Lsm2p-8p complex. To understand the function of Lsm1p, we constructed a series of deletion and point mutants of the LSM1 gene and examined their phenotypes. These studies revealed the following. (i) Integrity of the Lsm1p-7p complex is important for its mRNA decay function since mutations affecting the predicted inter-subunit interaction surfaces of Lsm1p lead to impairment of mRNA decay. (ii) Interactions between Lsm1p and mRNA are necessary for the activation of decapping by the Lsm1p-7p complex. However, even when these interactions are disrupted, the Lsm1p-7p complex could localize to the P-bodies. (iii) 3' end protection could be indicative of the binding of the Lsm1p-7p complex to the mRNA prior to activation of decapping since all the mutants defective in mRNA 3' end protection were also blocked in mRNA decay. (iv) In addition to the Sm domain the C-terminal domain of Lsm1p is also important for mRNA decay function.

Key Words: Lsm1, Sm-like, decapping, decay, mRNA




This article has been cited by other articles:


Home page
Genes Dev.Home page
C. J. Wilusz and J. Wilusz
New ways to meet your (3') end oligouridylation as a step on the path to destruction
Genes & Dev., January 1, 2008; 22(1): 1 - 7.
[Full Text] [PDF]


Home page
Genes Dev.Home page
T. E. Mullen and W. F. Marzluff
Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'
Genes & Dev., January 1, 2008; 22(1): 50 - 65.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
M. P. Spiller, M. A. M. Reijns, and J. D. Beggs
Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes
J. Cell Sci., December 15, 2007; 120(24): 4310 - 4320.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
R. Lotan, V. Goler-Baron, L. Duek, G. Haimovich, and M. Choder
The Rpb7p subunit of yeast RNA polymerase II plays roles in the two major cytoplasmic mRNA decay mechanisms
J. Cell Biol., September 24, 2007; 178(7): 1133 - 1143.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
A. Chowdhury, J. Mukhopadhyay, and S. Tharun
The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs
RNA, July 1, 2007; 13(7): 998 - 1016.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
D. Teixeira and R. Parker
Analysis of P-Body Assembly in Saccharomyces cerevisiae
Mol. Biol. Cell, June 1, 2007; 18(6): 2274 - 2287.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
V. Stribinskis and K. S. Ramos
Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies
Nucleic Acids Res., February 28, 2007; 35(4): 1301 - 1311.
[Abstract] [Full Text] [PDF]