title: The MYST histone acetyltransferases are essential for gametophyte development in Arabidopsis.
abstract: BACKGROUND
  Histone acetyltransferases (HATs) play critical roles in the regulation of chromatin structure and gene expression. Arabidopsis genome contains 12 HAT genes, but the biological functions of many of them are still unknown. In this work, we studied the evolutionary relationship and cellular functions of the two Arabidopsis HAT genes homologous to the MYST family members.
  
  
  RESULTS
  An extensive phylogenetic analysis of 105 MYST proteins revealed that they can be divided into 5 classes, each of which contains a specific combination of protein modules. The two Arabidopsis MYST proteins, HAM1 and HAM2, belong to a "green clade", clearly separated from other families of HATs. Using a reverse genetic approach, we show that HAM1 and HAM2 are a functionally redundant pair of genes, as single Arabidopsis ham1 and ham2 mutants displayed a wild-type phenotype, while no double mutant seedling could be recovered. Genetic analysis and cytological study revealed that ham1ham2 double mutation induced severe defects in the formation of male and female gametophyte, resulting in an arrest of mitotic cell cycle at early stages of gametogenesis. RT-PCR experiments and the analysis of transgenic plants expressing the GUS reporter gene under the HAM1 or the HAM2 promoter showed that both genes displayed an overlapping expression pattern, mainly in growing organs such as shoots and flower buds.
  
  
  CONCLUSIONS
  The work presented here reveals novel properties for MYST HATs in Arabidopsis. In addition to providing an evolutionary relationship of this large protein family, we show the evidence of a link between MYST and gamete formation as previously suggested in mammalian cells. A possible function of the Arabidopsis MYST protein-mediated histone acetylation during cell division is suggested.
authors.affiliation: Institut de Biotechnologie des Plantes, CNRS UMR8618, Université Paris-sud XI, 91405 Orsay, France. david.latrasse@u-psud.fr
authors.forename: David
authors.initials: D
authors.lastname: Latrasse
authors.forename: Moussa
authors.initials: M
authors.lastname: Benhamed
authors.forename: Yves
authors.initials: Y
authors.lastname: Henry
authors.forename: Séverine
authors.initials: S
authors.lastname: Domenichini
authors.forename: Wanhui
authors.initials: W
authors.lastname: Kim
authors.forename: Dao-Xiu
authors.initials: DX
authors.lastname: Zhou
authors.forename: Marianne
authors.initials: M
authors.lastname: Delarue
mesh_terms: D017360:Arabidopsis / Q000166:cytology / Q000196:embryology* / Q000201:enzymology* / Q000235:genetics; D004269:DNA, Bacterial / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D005854:Germ Cells / Q000166:cytology / Q000201:enzymology*; D005966:Glucuronidase / Q000378:metabolism; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016254:Mutagenesis, Insertional; D009154:Mutation / Q000235:genetics; D010641:Phenotype; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D004269:DNA, Bacterial; D012333:RNA, Messenger; C036483:T-DNA; D051548:Histone Acetyltransferases; D005966:Glucuronidase