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Related Experiment Videos

SAM domains: uniform structure, diversity of function.

Chongwoo A Kim1, James U Bowie

  • 1Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, Boyer Hall, 611 Charles E. Young Drive E, UCLA, Los Angeles, CA 90095-1570, USA.

Trends in Biochemical Sciences
|December 9, 2003
PubMed
Summary
This summary is machine-generated.

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Sterile alpha motif (SAM) domains, known for protein interactions, can unexpectedly bind RNA. This discovery complicates bioinformatic analysis of these protein families.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Sterile alpha motif (SAM) domains are recognized for their versatile protein-protein interaction capabilities.
  • These domains participate in various self-association architectures and interact with numerous non-SAM domain proteins.

Purpose of the Study:

  • To investigate the functional repertoire of SAM domains beyond protein interactions.
  • To explore novel functions associated with SAM domain proteins.

Main Methods:

  • Literature review and analysis of existing protein interaction databases.
  • Bioinformatic analysis of protein sequences and structures.

Main Results:

  • Identified a novel, unanticipated function for certain SAM domains: RNA binding.

Related Experiment Videos

  • Documented diverse functional roles within the homologous SAM domain protein family.

    • Conclusions:

    • The discovery of RNA-binding capability in SAM domains expands their known functional scope.
    • This functional heterogeneity poses challenges for accurate bioinformatic function prediction and assignment.