title: A maize histone deacetylase and retinoblastoma-related protein physically interact and cooperate in repressing gene transcription.
abstract: In mammalian cells the product of the human retinoblastoma tumour suppressor gene (pRb) can recruit Rpd3-like histone deacetylases to repress transcription. In this study, we investigated whether this mechanism might also be relevant in plants and found both conserved and distinct features. The expression profiles of the Zea mays Rpd3-type histone deacetylase (ZmRpd3I) and the retinoblastoma-related (ZmRBR1) homologues were analysed during endosperm development. GST pull-down and immunoprecipitation experiments showed a physical interaction between ZmRBRI and ZmRpd3I. Because ZmRpd3I lacks a LXCXE motif, conserved in several pRb-interacting proteins, we have mapped the amino acid domains involved in the ZmRBR1/ZmRpd3I interaction. Furthermore, we observed that ZmRbAp1, a maize member of the MSI/RbAp family, facilitated this protein interaction. Co-transformations of tobacco protoplasts with plasmids expressing ZmRBRI and ZmRpd3I showed that the two proteins cooperate in repressing gene transcription. Our findings represent the first indication that in plants a regulator of important biological processes, ZmRBRI, can recruit a histone deacetylase, ZmRpd3I, to control gene transcription.
authors.affiliation: Istituto Sperimentale per la Cerealicoltura, Sez. Bergamo, Via Stezzano 24, 24126 Bergamo, Italy. rossi@iscbg.it
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Rossi
authors.forename: Sabrina
authors.initials: S
authors.lastname: Locatelli
authors.forename: Chiara
authors.initials: C
authors.lastname: Lanzanova
authors.forename: M Beatrice
authors.initials: MB
authors.lastname: Boniotti
authors.forename: Serena
authors.initials: S
authors.lastname: Varotto
authors.forename: Alexandra
authors.initials: A
authors.lastname: Pipal
authors.forename: Maria
authors.initials: M
authors.lastname: Goralik-Schramel
authors.forename: Alexandra
authors.initials: A
authors.lastname: Lusser
authors.forename: Christiane
authors.initials: C
authors.lastname: Gatz
authors.forename: Crisanto
authors.initials: C
authors.lastname: Gutierrez
authors.forename: Mario
authors.initials: M
authors.lastname: Motto
mesh_terms: D001665:Binding Sites / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D002868:Chromosomal Proteins, Non-Histone; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism*; D015151:Immunoblotting; D017403:In Situ Hybridization; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012639:Seeds / Q000235:genetics / Q000254:growth & development; D014158:Transcription, Genetic / Q000235:genetics*; D003313:Zea mays / Q000235:genetics / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D010940:Plant Proteins; C107938:RRB1 protein, Zea mays; C432691:RbAp1 protein, Zea mays; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D006655:Histone Deacetylases