Plant SAM-Domain Proteins Start to Reveal Their Roles

Trends Plant Sci. 2017 Aug;22(8):718-725. doi: 10.1016/j.tplants.2017.06.006. Epub 2017 Jun 28.

Abstract

Proteins often act in complexes assembled via protein-protein interaction domains. The sterile alpha motif (SAM) domain is one of the most prominent interaction domains in animals and is present in proteins of diverse functions. This domain allows head-to-tail closed oligomerisation or polymer formation resulting in homo- and/or heterocomplexes that have been shown to be important for proper protein localisation and function. In plants this domain is also present but has been poorly studied except for recent studies on the LEAFY floral regulator and the tRNA import component (TRIC)1/2 proteins. Here we catalogue SAM domain-containing proteins from arabidopsis (Arabidopsis thaliana), compare plant and other eukaryotic SAM domains, and perform homology modelling to probe plant SAM domain interaction capabilities.

Keywords: LEAFY; TRIC1/2; arabidopsis; oligomerisation; sterile alpha motif.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / genetics*
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Models, Molecular*
  • Models, Structural
  • Protein Interaction Domains and Motifs
  • Sequence Alignment
  • Sterile Alpha Motif*

Substances

  • Arabidopsis Proteins