title: mRNA regulation by Puf domain proteins.
abstract: Puf domain proteins bind specific sequences in mRNAs to regulate their translation or stability, or both. Neither the mechanism of their action nor the identities of targeted mRNAs have been well defined. Recent work suggests that Puf proteins generally act by recruiting Pop2, a deadenylation enzyme that is part of a large complex. Recent work from a separate group defines a subset of the Drosophila transcriptome that is bound by the fly Puf protein, Pumilio. Together, these papers substantially increase our understanding of the biology of the Puf family of mRNA regulators.
authors.affiliation: Howard Hughes Medical Institute and Duke University Medical School, Durham, NC 27710, USA. rwharton@duke.edu
authors.forename: Robin P
authors.initials: RP
authors.lastname: Wharton
authors.forename: Aneel K
authors.initials: AK
authors.lastname: Aggarwal
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D015252:Deoxyribonucleases, Type II Site-Specific / Q000235:genetics / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D011061:Poly A / Q000378:metabolism; D011485:Protein Binding; D020871:RNA Stability; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D018797:Cell Cycle Proteins; D029721:Drosophila Proteins; C449502:MPT5 protein, S cerevisiae; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; C074333:pum protein, Drosophila; D011061:Poly A; C078657:CCR4 protein, S cerevisiae; D012260:Ribonucleases; C445084:mRNA deadenylase; C079009:POP2 protein, S cerevisiae; C037725:SCEI protein, S cerevisiae; D015252:Deoxyribonucleases, Type II Site-Specific