A novel function for the Sm proteins in germ granule localization during C-elegans embryogenesis

被引:48
作者
Barbee, SA
Lublin, AL
Evans, TC
机构
[1] Univ Colorado, Hlth Sci Ctr, Program Cell & Dev Biol, Denver, CO 80262 USA
[2] Univ Colorado, Hlth Sci Ctr, Dept Cellular & Struct Biol, Denver, CO 80262 USA
基金
美国国家科学基金会;
关键词
D O I
10.1016/S0960-9822(02)01111-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
General mRNA processing factors are traditionally thought to function only in the control of global gene expression. Here we show that the Sm proteins, core components of the splicesome, also regulate germ granules during early C. elegans development. Germ granules are large cytoplasmic particles that localize to germ cells and their precursors during embryogenesis of diverse organisms [1]. In C. elegrans, germ granules, called P granules, are segregated to the germline precursor cells during embryogenesis by asymmetric cell division, and they remain in germ cells at all stages of development [2]. We found that at least some Sm proteins are components of P granules. Moreover, disruption of Sm activity caused defects in P granule localization to the germ cell precursors during early embryogenesis. In contrast, loss of other splicing factor activities had no effect on germ granule control in the embryo. These observations suggest that the Sm proteins control germ granule integrity and localization in the early C. elegans embryo and that this role is independent of pre-mRNA splicing. Thus, a highly conserved splicing factor may have been adapted to control both snRNP biogenesis and the localization of components important for germ cell function.
引用
收藏
页码:1502 / 1506
页数:5
相关论文
共 34 条
[1]  
Amiri A, 2001, DEVELOPMENT, V128, P3899
[2]   Functioning of the Drosophila integral U1/U2 protein Snf independent of U1 and U2 small nuclear ribonucleoprotein particles is revealed by snf+ gene dose effects [J].
Cline, TW ;
Rudner, DZ ;
Barbash, DA ;
Bell, M ;
Vutien, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (25) :14451-14458
[3]   TRANSLATIONAL CONTROL OF MATERNAL GLP-1 MESSENGER-RNA ESTABLISHES AN ASYMMETRY IN THE C-ELEGANS EMBRYO [J].
EVANS, TC ;
CRITTENDEN, SL ;
KODOYIANNI, V ;
KIMBLE, J .
CELL, 1994, 77 (02) :183-194
[4]   AN ESSENTIAL SIGNALING ROLE FOR THE M3G CAP IN THE TRANSPORT OF U1 SNRNP TO THE NUCLEUS [J].
FISCHER, U ;
LUHRMANN, R .
SCIENCE, 1990, 249 (4970) :786-790
[5]   NUCLEOCYTOPLASMIC TRANSPORT OF U SNRNPS - DEFINITION OF A NUCLEAR LOCATION SIGNAL IN THE SM CORE DOMAIN THAT BINDS A TRANSPORT RECEPTOR INDEPENDENTLY OF THE M3G CAP [J].
FISCHER, U ;
SUMPTER, V ;
SEKINE, M ;
SATOH, T ;
LUHRMANN, R .
EMBO JOURNAL, 1993, 12 (02) :573-583
[6]   Thirteen anti-Sm monoclonal antibodies immunoprecipitate the three cytoplasmic snRNP core protein precursors in six distinct subsets [J].
Fury, M ;
Andersen, J ;
Ponda, P ;
Aimes, R ;
Zieve, GW .
JOURNAL OF AUTOIMMUNITY, 1999, 12 (02) :91-100
[7]   Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport [J].
Hachet, O ;
Ephrussi, A .
CURRENT BIOLOGY, 2001, 11 (21) :1666-1674
[8]   THE TRIMETHYLGUANOSINE CAP STRUCTURE OF U1 SNRNA IS A COMPONENT OF A BIPARTITE NUCLEAR TARGETING SIGNAL [J].
HAMM, J ;
DARZYNKIEWICZ, E ;
TAHARA, SM ;
MATTAJ, IW .
CELL, 1990, 62 (03) :569-577
[9]   Functions of Lsm proteins in mRNA degradation and splicing [J].
He, WH ;
Parker, R .
CURRENT OPINION IN CELL BIOLOGY, 2000, 12 (03) :346-350
[10]   SNRNP SM PROTEINS SHARE 2 EVOLUTIONARILY CONSERVED SEQUENCE MOTIFS WHICH ARE INVOLVED IN SM PROTEIN-PROTEIN INTERACTIONS [J].
HERMANN, H ;
FABRIZIO, P ;
RAKER, VA ;
FOULAKI, K ;
HORNIG, H ;
BRAHMS, H ;
LUHRMANN, R .
EMBO JOURNAL, 1995, 14 (09) :2076-2088