The PGL family proteins associate with germ granules and function redundantly in Caenorhabditis elegans germline development
The PGL family proteins associate with germ granules and function redundantly in Caenorhabditis elegans germline development
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DOI:
10.1534/genetics.103.023093
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发表时间:
2004-06-01
期刊:
影响因子:
3.3
通讯作者:
Strome, S
中科院分区:
文献类型:
--
作者:
Kawasaki, L;Amiri, A;Strome, S
PGL-1 is a constitutive protein component of C. elegans germ granules, also known as P granules. Maternally supplied PGL-1 is essential for germline development but only at elevated temperature, raising the possibility that redundant factors provide sufficient function at lower temperatures. We have identified two PGLA-related proteins, PGL-2 and PGL-3, by sequence analysis of the C. elegans genome and by a yeast two-hybrid screen for proteins that interact with PGL-1. PGL-3 is associated with P granules at all stages of development, while PGL-2 is associated with 11 granules only during postembryonic development. All three PGL proteins interact with each other in vitro. Furthermore, PGL-1 and PGL-3 are co-immuno-precipitated from embryo extracts, indicating that they are indeed in the same protein complex in vivo. Nevertheless, each PGL. protein localizes to P granules independently of the other two. pgl-2 or pgl-3 single-mutant worms do not show obvious defects in germline development. However, pgl-1; pgl-3 (but not pgl-2; pgl-1) double-mutant hermaphrodites and males show significantly enhanced sterility at all temperatures, compared to pgl-1 alone. Mutant hermaphrodites show defects in germline proliferation and in production of healthy gametes and viable embryos. Our findings demonstrate that both PGL-2 and PGL-3 are components of P granules, both interact with PGL-1, and at least PGL-3 functions redundantly with PGL-1 to ensure fertility in both sexes of C. elegans.