Plant SET domain-containing proteins: structure, function and regulation

0307207 - ÚEB 2008 RIV NL eng J - Článek v odborném periodiku
Ng, D.W.K. - Wang, T. - Chandrasekharan, M.B. - Aramayo, R. - Kertbundit, Sunee - Hall, T.C.
Plant SET domain-containing proteins: structure, function and regulation.
[Proteiny SET-domén u rostlin: struktura, funkce a regulace.]
Biochimica Et Biophysica Acta-Gene Structure and Expression. Roč. 1769, 5-6 (2007), s. 316-329. ISSN 0167-4781
Výzkumný záměr: CEZ:AV0Z50380511
Klíčová slova: arabidopsis SET genes * alternative splicing * epigenetics
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 1.704, rok: 2007

Modification of the historic proteins that form the core around which chromosomal DNA is looped has profound epigenetic effects on the accessibility of the associated DNA for transcription, replication and repair. The SET domain is now recognized as generally having methyltransferase activity targeted to specific lysine residues of histone H3 or H4. There is considerable sequence conservation within the SET domain and within its flanking regions. Previous reviews have shown that SET proteins from Arabidopsis and maize fall into five classes according to their sequence and domain architectures. These classes generally reflect specificity for a particular substrate. SET proteins from rice were found to fall into similar groupings, strengthening the merit of the approach taken. Two additional classes, VI and VII, were established that include proteins with truncated/ interrupted SET domains. Diverse mechanisms are involved in shaping the function and regulation of SET proteins. These include protein-protein interactions through both intra- and inter-molecular associations that are important in plant developmental processes, such as flowering time control and embryogenesis. Alternative splicing that can result in the generation of two to several different transcript isoforms is now known to be widespread. An exciting and tantalizing question is whether, or how, this alternative splicing affects gene function. For example, it is conceivable that one isoform may debilitate methyltransferase function whereas the other may enhance it, providing an opportunity for differential regulation. The review concludes with the speculation that modulation of SET protein function is mediated by antisense or sense-antisense RNA.

O SET-doméně je dnes známé, že má methyltransferasovou aktivitu zaměřenou na specifická rezidua lysinu v histonech H3 a H4. V tomto přehledu jsou charakterizovány jednotlivé třídy rostliných SET proteinů na základě jejich sekvence, doménové architektury, biochemických funkcí i alternativního střihu RNA. Diskutován je i vliv antisence or sense-entisense RNA na jejich funkce.
Trvalý link: http://hdl.handle.net/11104/0160038