title: Complex expression pattern of the Barth syndrome gene product tafazzin in human cell lines and murine tissues.
abstract: Tafazzins, a group of proteins that are defective in patients with Barth syndrome, are produced by alternate splicing of the gene G4.5 or TAZ. RT-PCR and transcription-coupled in vitro translation analysis were undertaken to determine the expression of alternatively spliced TAZ mRNA in mouse tissues and human cell lines. Only two tafazzin transcripts, both lacking exon 5, were expressed in murine tissues, whereas four tafazzin transcripts, all lacking exon 5, were observed in human umbilical vein vascular endothelial cells and U937 human monoblasts indicating a species-specific difference in the expression of TAZ mRNAs in mouse and humans. Only TAZ lacking exon 5 was expressed in murine heart. Differentiation of U937 human monoblasts into macrophages did not alter expression of the tafazzin transcripts indicating that TAZ expression is independent of monocyte differentiation. Cloning and in vitro expression of both murine and human tafazzin cDNA revealed two prominent protein bands that corresponded to the expected sizes of alternative translation. A novel fifth motif, identified as critical for the glycerolphosphate acyltransferase family, was observed in human tafazzin. The presence of a mutation in this region in Barth syndrome patients indicates that this motif is essential for tafazzin function.
authors.affiliation: Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, MB R3E 0T6, Canada.
authors.forename: Biao
authors.initials: B
authors.lastname: Lu
authors.forename: Marguerite R
authors.initials: MR
authors.lastname: Kelher
authors.forename: Douglas P
authors.initials: DP
authors.lastname: Lee
authors.forename: Tal M
authors.initials: TM
authors.lastname: Lewin
authors.forename: Rosalind A
authors.initials: RA
authors.lastname: Coleman
authors.forename: Patrick C
authors.initials: PC
authors.lastname: Choy
authors.forename: Grant M
authors.initials: GM
authors.lastname: Hatch
mesh_terms: D000217:Acyltransferases; D017398:Alternative Splicing / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D002454:Cell Differentiation / Q000502:physiology; D002478:Cells, Cultured; D005786:Gene Expression Regulation / Q000235:genetics / Q000502:physiology*; D040181:Genetic Diseases, X-Linked / Q000235:genetics / Q000378:metabolism; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000378:metabolism*; D006801:Humans; D008264:Macrophages / Q000166:cytology / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D014018:Tissue Distribution; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*
chemical_list: D011506:Proteins; D012333:RNA, Messenger; D014157:Transcription Factors; D000217:Acyltransferases; C486363:tafazzin protein, mouse; C108675:TAFAZZIN protein, human; D005992:Glycerol-3-Phosphate O-Acyltransferase