A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study

Authors

  • Michael Hisbergues,

    1. Laboratoire de Chimie bacterienne—Centre National de la Recherche Scientifique, F13402 Marseilles Cedex 20, France
    2. Institut für Biologie, Humboldt Universität, D-10115 Berlin, Germany
    Current affiliation:
    1. Humboldt Universität, Institut für Biologie (Genetik), Chausseestrasse 117, D10115 Berlin, Germany.
    Search for more papers by this author
  • Chrysanthe G. Gaitatzes,

    1. Biomolecular Engineering Research Center, College of Engineering, Boston University, Boston, Massachusetts 02215, USA
    Search for more papers by this author
  • Françoise Joset,

    Corresponding author
    1. Laboratoire de Chimie bacterienne—Centre National de la Recherche Scientifique, F13402 Marseilles Cedex 20, France
    • Françoise Joset, LCB-CNRS, 31 Chemin J. Aiguier, F13402 Marseilles Cedex 20, France; fax: 33-0-4-91-71-89-14.
    Search for more papers by this author
  • Sylvie Bedu,

    1. Laboratoire de Chimie bacterienne—Centre National de la Recherche Scientifique, F13402 Marseilles Cedex 20, France
    Search for more papers by this author
  • Temple F. Smith

    1. Biomolecular Engineering Research Center, College of Engineering, Boston University, Boston, Massachusetts 02215, USA
    Search for more papers by this author

Abstract

Synechocystis PCC6803 possesses several open reading frames encoding putative WD-repeat proteins. One, the Hat protein, is involved in the control of a high-affinity transport system for inorganic carbon that is active when the cells are grown under a limiting concentration of this carbon substrate. The protein is composed of two major domains separated by a hydrophobic linker region of 20 amino acid residues. The N-terminal domain of Hat has no homolog in standard databases and does not display any particular structural features. Eleven WD repeats have been identified in the C-terminal moiety. The region encompassing the four terminal WD repeats is essential for growth under a limiting inorganic carbon regime. The region encompassing the two most terminal WD repeats is required for the activity of the high-affinity transport system. However, because the Hat protein is located in the thylakoids, it should not be itself an element of the transport system. The structural organization of the WD-containing domain of Hat was modeled from the crystal structure of the G protein β subunit (with seven WD repeats) and of hemopexin (a structural analog with four blades). Functional and structural data argue in favor of an organization of the Hat WD moiety in two subdomains of seven and four WD repeats. The C-terminal 4-mer subdomain might interact with another, yet unknown, protein/peptide. This interaction could be essential in modulating the stability of the 4-mer structure and, thus, the accessibility of this subdomain, or at least of the region encompassing the last two WD repeats.

Ancillary