[Seminars] PSB event reminder

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Calendar Name: seminars
Scheduled for: Thursday, November 17 2011, 11:00 - 12:30
Event text:    Prof Reidunn Birgitta Aalen
	       
	       Department of Molecular Biosciences
	       University of Oslo 
	       
	       NORWAY
Details:       "Matching ligands with receptors and readers with
	       writers of the histone code"
	       
	       ABSTRACT
	       Multicellular organisms are dependent on mechanisms of
	       cell-to-cell communication and tight control of gene
	       expression to ensure that each cell attains the correct
	       function in the organism as a whole. My group is
	       elucidating these mechanism by two approaches – our aim
	       is 1) to match putative peptide ligands with receptors,
	       and 2) to understand how histone lysine
	       methyltransferases (HKMTases) influence chromatin
	       structure: 1) Although there are about thousand genes in
	       Arabidopsis encoding putative secreted peptide ligands,
	       and more than four hundred encoding receptor-like
	       kinases (RLKs), less than a dozen peptide ligands –
	       receptor pairs influencing development have been
	       identified to date (Butenko et al, Trends Plant Sci,
	       2009). One of these modules is the INFLORESCENCE
	       DEFICIENT IN ABSCISSION (IDA) peptide signaling through
	       the leucine-rich repeat (LRR) RLKs HAESA and HAESA-LIKE
	       2 to control floral organ abscission after pollination
	       has taken place (Stenvik et al, Plant Cell, 2008; Shi et
	       al, Plant Cell, 2011). We have suggested that IDA as
	       well as IDA-LIKE peptides, which share a conserved
	       proline-rich C-terminal motif, signal through HAESA-LIKE
	       LRR-RLKs also to control other cell separation processes
	       in plants.  2) Ten years ago we identified the near to
	       forty Arabidopsis genes encoding SET-domain proteins,
	       which are putative HKMTases (Baumbusch et al, Nucl Acids
	       Res, 2001; Thorstensen et al, BBA, 2011). Recently we
	       have demonstrated the importance of co-domains in such
	       proteins – the WIYLD domain of the H3K9me2/me3 HKMTase
	       SUVR4 is a ubiquitin-binding domain that can regulate
	       the product specificity of SUVR4 in relation to its
	       suppression of transposon activity (Thorstensen et al,
	       PLoS Genetics, 2011); and the CW domain of the
	       H3K36me2/me3 HKMTase ASHH2 is a novel reader of H3K4me
	       assisting in ASHH2’s global involvement in maintenance
	       of tissue-specific gene expression 
	       (Hoppmann et al. EMBO J, 2011).

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