title: Heat shock disassembles the nucleolus and inhibits nuclear protein import and poly(A)+ RNA export.
abstract: Heat shock causes major positive and negative changes in gene expression, drastically alters the appearance of the nucleolus and inhibits rRNA synthesis. We here show that it causes many yeast nucleolar proteins, including the fibrillarin homolog Nop1p, to relocate to the cytoplasm. Relocation depends on several proteins implicated in mRNA transport (Mtrps) and is reversible. Two observations indicate, surprisingly, that disassembly results from a reduction in Ssa protein (Hsp70) levels: (i) selective depletion of Ssa1p leads to disassembly of the nucleolus; (ii) preincubation at 37 degrees C protects the nucleolus against disassembly by heat shock, unless expression of Ssa proteins is specifically inhibited. We observed that heat shock or reduction of Ssa1p levels inhibits protein import into the nucleus and therefore we propose that inhibition of import leads to disassembly of the nucleolus. These observations provide a simple explanation of the effects of heat shock on the anatomy of the nucleolus and rRNA transcription. They also extend understanding of the path of nuclear export. Since a number of nucleoplasmic proteins also relocate upon heat shock, these observations can provide a general mechanism for regulation of gene expression. Relocation of the hnRNP-like protein Mtr13p (= Npl3p, Nop3p), explains the heat shock sensitivity of export of average poly(A)+ RNA. Strikingly, Hsp mRNA export appears not to be affected.
authors.affiliation: Department of Pathology and Cell Biology Program, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Liu
authors.forename: S
authors.initials: S
authors.lastname: Liang
authors.forename: A M
authors.initials: AM
authors.lastname: Tartakoff
mesh_terms: D002466:Cell Nucleolus / Q000502:physiology* / Q000648:ultrastructure; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D005656:Fungal Proteins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000096:biosynthesis / Q000378:metabolism*; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D006358:Hot Temperature; D007700:Kinetics; D008954:Models, Biological; D009687:Nuclear Proteins / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*; D020718:Ribonucleoproteins, Small Nucleolar; D012441:Saccharomyces cerevisiae / Q000502:physiology* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins; D013104:Spheroplasts / Q000502:physiology
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D034441:Heterogeneous-Nuclear Ribonucleoproteins; C064793:NOP1 protein, S cerevisiae; D009687:Nuclear Proteins; D012333:RNA, Messenger; D012261:Ribonucleoproteins; D020718:Ribonucleoproteins, Small Nucleolar; D029701:Saccharomyces cerevisiae Proteins; C047458:fibrillarin