Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress.
Multiple KH-domain proteins, collectively known as vigilins, are evolutionarily highly conserved proteins that are present in eukaryotic organisms from yeast to metazoa. Proposed roles for vigilins include chromosome segregation, messenger RNA (mRNA) metabolism, translation and tRNA transport. As a step toward understanding its biological function, we have identified the fission yeast vigilin, designated Vgl1, and have investigated its role in cellular response to environmental stress. Unlike its counterpart in Saccharomyces cerevisiae, we found no indication that Vgl1 is required for the maintenance of cell ploidy in Schizosaccharomyces pombe. Instead, Vgl1 is required for cell survival under thermal stress, and vgl1Δ mutants lose their viability more rapidly than wild-type cells when incubated at high temperature. As for Scp160 in S. cerevisiae, Vgl1 bound polysomes accumulated at endoplasmic reticulum (ER) but in a microtubule-independent manner. Under thermal stress, Vgl1 is rapidly relocalized from the ER to cytoplasmic foci that are distinct from P-bodies but contain stress granule markers such as poly(A)-binding protein and components of the translation initiation factor eIF3. Together, these observations demonstrated in S. pombe the presence of RNA granules with similar composition as mammalian stress granules and identified Vgl1 as a novel component that required for cell survival under thermal stress.
Wen
Wei-Ling
WL
Division of Molecular and Genomic Medicine, National Health Research Institutes, 35 Keyan Road, Zhunan Town, Miaoli County 350, Taiwan.
Stevenson
Abigail L
AL
Wang
Chun-Yu
CY
Chen
Hsiang-Ju
HJ
Kearsey
Stephen E
SE
Norbury
Chris J
CJ
Watt
Stephen
S
Bähler
Jürg
J
Wang
Shao-Win
SW
D003594:Cytoplasmic Granules / Q000737:chemistry*; D004721:Endoplasmic Reticulum / Q000737:chemistry; D015870:Gene Expression; D006358:Hot Temperature; D008870:Microtubules / Q000502:physiology; D009154:Mutation; D011123:Polyploidy; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins / Q000032:analysis; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis; D012568:Schizosaccharomyces / Q000235:genetics / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D013312:Stress, Physiological
D016601:RNA-Binding Proteins; C097262:SCP160 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; C554521:Vgl1 protein, S pombe