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

Danny W-K Ng1, Tao Wang, Mahesh B Chandrasekharan

  • 1Institute of Developmental and Molecular Biology and Department of Biology, Texas A&M University, College Station, TX 77843-3155, USA.

Biochimica Et Biophysica Acta
|May 22, 2007
PubMed
Summary
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Histone modifications by SET domain proteins impact DNA accessibility for crucial cellular processes. Alternative splicing of these proteins may offer differential regulation of their methyltransferase activity.

Area of Science:

  • Plant molecular biology
  • Epigenetics
  • Chromatin biology

Background:

  • Histone modifications are key epigenetic regulators influencing DNA accessibility.
  • SET domain proteins are methyltransferases targeting specific histone lysine residues.
  • Sequence conservation in SET domains suggests functional relatedness.

Purpose of the Study:

  • To review and classify plant SET domain proteins based on sequence and domain architecture.
  • To explore regulatory mechanisms of SET protein function, including protein-protein interactions and alternative splicing.
  • To investigate the potential impact of alternative splicing on SET protein methyltransferase activity.

Main Methods:

  • Comparative sequence analysis of SET proteins across plant species (Arabidopsis, maize, rice).

Related Experiment Videos

  • Classification of SET proteins into distinct groups based on domain structure.
  • Review of literature on protein-protein interactions and alternative splicing in SET protein regulation.

    • Main Results:

    • Plant SET proteins were classified into seven groups, with Classes VI and VII including those with truncated/interrupted SET domains.
    • Protein-protein interactions are implicated in regulating plant development via SET proteins.
    • Alternative splicing is widespread and may lead to isoforms with differential methyltransferase functions.

    Conclusions:

    • The classification of plant SET proteins provides a framework for understanding their substrate specificity.
    • Diverse regulatory mechanisms, including alternative splicing, modulate SET protein function.
    • Antisense or sense-antisense RNA may play a role in regulating SET protein activity.