- Seminars - maillist.psb.ugent.be

PSB event reminder
by contact＠psb.vib-ugent.be 15 Nov '11

15 Nov '11

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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Seminar Prof Reidunn Birgitta Aalen
by Delphine Verspeel 08 Nov '11

08 Nov '11

You are receiving this e-mail because you subscribed to our seminars announcements and reminders service at <https://maillist.psb.ugent.be/mailman/listinfo/seminars> https://maillist.psb.ugent.be/mailman/listinfo/seminars. If you do not wish to receive this information anymore, please unsubscribe from future mailings at <https://maillist.psb.ugent.be/mailman/options/seminars> https://maillist.psb.ugent.be/mailman/options/seminars. cid:946540515@15122008-0D1C PSB cid:946540515@15122008-0D23 VIB - Department of Plant Systems Biology Technologiepark 927 B - 9052 Gent/Zwijnaarde Phone: +32 9 33 13 800 Fax: +32 9 33 13 809 Http://www.psb.vib-ugent.be

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PSB event reminder
by contact＠psb.vib-ugent.be 07 Nov '11

07 Nov '11

Calendar Name: seminars Scheduled for: Monday, November 7 2011, 11:00 - 12:30 Event text: Prof Peter Tompa VIB Department of Structural Biology Vrije Universiteit Brussel Brussel BELGIUM Details: �Intrinsically disordered proteins in cellular function and disease� ABSTRACT Peter Tompa1,2 1VIB Department of Structural Biology, Brussels and 2Institute of Enzymology, Budapest Our traditional view of proteins is rooted in the notion that a well-defined three-dimensional structure is the prerequisite of their function. The evidence is steadily growing, however, that for a significant fraction of the proteome the functionally relevant state is not structured [1,2]. This recognition has called for the extension of the protein structure-function paradigm to encompass such proteins and protein domains, now termed intrinsically unstructured, intrinsically disordered (IDPs) or natively unfolded. Here the current state of this rapidly advancing field is surveyed [3]. It is shown that such proteins are common in living organisms and play important roles in the regulation of key cellular processes of signaling and transcription. It will be shown that we have multiple experimental techniques at our disposal for the characterization of the structural ensemble of IDPs, and also that structural disorder provides advantages so that IDPs often surpass globular proteins in terms of functional specificity, versatility, speed and control [4]. Because of their important functions, however, IDPs are also often involved in disease, such as cancer and neurodegeneration. Thus, it is argued that understanding this structural phenomenon at atomic resolution not only represents a novel challenge for extending the structure-function paradigm, but also presents novel targets and raises new hope for drug discovery [5]. [1] Tompa, P. (2002) Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533. [2] Tompa, P. (2009) Structure and function of intrinsically disordered proteins, CRC Press (Taylor and Francis Group), Boca Raton, Fl. [3] Tompa, P. (2011) Unstructural biology coming of age. Curr. Opin. Struct. Biol. 21, 419-25. [4] Kovacs, D., Kalmar, E., Torok, Z. and Tompa, P. (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol. 147, 381-90. [5] Metallo, S.J. (2010) Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol. 14, 481-8.

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PSB event reminder
by contact＠psb.vib-ugent.be 05 Nov '11

05 Nov '11

Calendar Name: seminars Scheduled for: Monday, November 7 2011, 11:00 - 12:30 Event text: Prof Peter Tompa VIB Department of Structural Biology Vrije Universiteit Brussel Brussel BELGIUM Details: �Intrinsically disordered proteins in cellular function and disease� ABSTRACT Peter Tompa1,2 1VIB Department of Structural Biology, Brussels and 2Institute of Enzymology, Budapest Our traditional view of proteins is rooted in the notion that a well-defined three-dimensional structure is the prerequisite of their function. The evidence is steadily growing, however, that for a significant fraction of the proteome the functionally relevant state is not structured [1,2]. This recognition has called for the extension of the protein structure-function paradigm to encompass such proteins and protein domains, now termed intrinsically unstructured, intrinsically disordered (IDPs) or natively unfolded. Here the current state of this rapidly advancing field is surveyed [3]. It is shown that such proteins are common in living organisms and play important roles in the regulation of key cellular processes of signaling and transcription. It will be shown that we have multiple experimental techniques at our disposal for the characterization of the structural ensemble of IDPs, and also that structural disorder provides advantages so that IDPs often surpass globular proteins in terms of functional specificity, versatility, speed and control [4]. Because of their important functions, however, IDPs are also often involved in disease, such as cancer and neurodegeneration. Thus, it is argued that understanding this structural phenomenon at atomic resolution not only represents a novel challenge for extending the structure-function paradigm, but also presents novel targets and raises new hope for drug discovery [5]. [1] Tompa, P. (2002) Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533. [2] Tompa, P. (2009) Structure and function of intrinsically disordered proteins, CRC Press (Taylor and Francis Group), Boca Raton, Fl. [3] Tompa, P. (2011) Unstructural biology coming of age. Curr. Opin. Struct. Biol. 21, 419-25. [4] Kovacs, D., Kalmar, E., Torok, Z. and Tompa, P. (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol. 147, 381-90. [5] Metallo, S.J. (2010) Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol. 14, 481-8.

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FW: Upcoming seminars November
by Delphine Verspeel 04 Nov '11

04 Nov '11

Dear all, Enclosed the updated list for November. Kind regards, Delphine From: Delphine Verspeel [mailto:despe@psb.ugent.be] Sent: woensdag 26 oktober 2011 17:24 To: 'meetings(a)psb.vib-ugent.be' Subject: Upcoming seminars November Dear all, Enclosed you can find our upcoming seminars for November. Kind regards, Delphine ____________________________________________ Delphine Verspeel Administrative Assistant VIB, Department of Plant Systems Biology Ghent University Technologiepark 927 9052 Gent Belgium Phone: +32/9/33.13.800 Fax: +32/33.13.809 Http://www.psb.ugent.be despe(a)psb.vib-ugent.be <mailto:nahau@psb.vib-ugent.be>

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Seminar Prof Peter Tompa
by Delphine Verspeel 27 Oct '11

27 Oct '11

You are receiving this e-mail because you subscribed to our seminars announcements and reminders service at <https://maillist.psb.ugent.be/mailman/listinfo/seminars> https://maillist.psb.ugent.be/mailman/listinfo/seminars. If you do not wish to receive this information anymore, please unsubscribe from future mailings at <https://maillist.psb.ugent.be/mailman/options/seminars> https://maillist.psb.ugent.be/mailman/options/seminars. cid:946540515@15122008-0D1C PSB cid:946540515@15122008-0D23 VIB - Department of Plant Systems Biology Technologiepark 927 B - 9052 Gent/Zwijnaarde Phone: +32 9 33 13 800 Fax: +32 9 33 13 809 Http://www.psb.vib-ugent.be

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Upcoming seminars November
by Delphine Verspeel 26 Oct '11

26 Oct '11

Dear all, Enclosed you can find our upcoming seminars for November. Kind regards, Delphine ____________________________________________ Delphine Verspeel Administrative Assistant VIB, Department of Plant Systems Biology Ghent University Technologiepark 927 9052 Gent Belgium Phone: +32/9/33.13.800 Fax: +32/33.13.809 Http://www.psb.ugent.be despe(a)psb.vib-ugent.be <mailto:nahau@psb.vib-ugent.be>

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PSB event reminder
by contact＠psb.vib-ugent.be 25 Oct '11

25 Oct '11

Calendar Name: seminars Scheduled for: Tuesday, October 25 2011, 14:00 - 15:30 Event text: Prof Susan R. Wessler Dept of Botany and Plant Sciences University of California Riverside USA Details: �The success strategies of transposable elements that diversify genomes� ABSTRACT Despite the widespread prevalence of transposable elements (TEs) in the genomes of higher eukaryotes, what is virtually unknown is how they are able to amplify to high copy numbers without being silenced and without killing their host. In this seminar I will discuss our recent studies on MITEs (miniature inverted repeat transposable elements), a type of class 2 element that was discovered in my laboratory 20 years ago as the most prevalent TE associated with plant genes. To understand how MITEs can attain high copy numbers, we succeeded in identifying a MITE, mPing, in the midst of rapid amplification throughout the genomes of several related rice strains. Nextgen sequencing technologies are being employed to determine mPing�s strategies for success and to understand how mPing impacts host transcription and generates phenotypic diversity.

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PSB event reminder
by contact＠psb.vib-ugent.be 23 Oct '11

23 Oct '11

Calendar Name: seminars Scheduled for: Tuesday, October 25 2011, 14:00 - 15:30 Event text: Prof Susan R. Wessler Dept of Botany and Plant Sciences University of California Riverside USA Details: �The success strategies of transposable elements that diversify genomes� ABSTRACT Despite the widespread prevalence of transposable elements (TEs) in the genomes of higher eukaryotes, what is virtually unknown is how they are able to amplify to high copy numbers without being silenced and without killing their host. In this seminar I will discuss our recent studies on MITEs (miniature inverted repeat transposable elements), a type of class 2 element that was discovered in my laboratory 20 years ago as the most prevalent TE associated with plant genes. To understand how MITEs can attain high copy numbers, we succeeded in identifying a MITE, mPing, in the midst of rapid amplification throughout the genomes of several related rice strains. Nextgen sequencing technologies are being employed to determine mPing�s strategies for success and to understand how mPing impacts host transcription and generates phenotypic diversity.

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PSB event reminder
by contact＠psb.vib-ugent.be 20 Oct '11

20 Oct '11

Calendar Name: seminars Scheduled for: Thursday, October 20 2011, 11:00 - 12:30 Event text: Prof Alain Goossens VIB, Dept. of Plant Systems Biology Ghent University Gent BELGIUM Details: "Jasmonates : Gatekeepers of the plant�s defense metabolite universe" ABSTRACT Across the plant kingdom, the jasmonate hormone steers the delicate balance between growth and the activation of defence programs, such as the production of bioactive secondary metabolites. The signaling machinery that established the function of jasmonates as regulators of (secondary) metabolism is conserved and installed early in the higher plant lineage. But, in spite of the similarities of many of the regulators, ultimately species-specific secondary metabolic pathways have evolved under jasmonate control. By using cutting-edge functional genomics tools, in combination with reverse genetics screenings, we try to identify the essential components acting in the jasmonate signalling network, in medicinal plants and in the model plant Arabidopsis thaliana. Such components can ultimately lead to the creation of new metabolic engineering tools that may improve the exploitation of the plant metabolic machinery. Surprisingly, the screens that we have performed not only allowed identifying positive regulators of jasmonate elicitation of metabolism but also revealed the existence of multiple 'safety breaks' that serve to optimize plant survival under stress conditions.

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