Identification of a novel prokaryotic HEAT-repeats-containing protein which interacts with a cyanobacterial IscA homolog

FEBS Lett. 2002 May 22;519(1-3):123-7. doi: 10.1016/s0014-5793(02)02736-9.


IscA homologs are known to be involved in iron-sulfur cluster formation in various organisms. Recombinant proteins of two IscA homologs from the cyanobacterium Synechocystis PCC 6803, designated SLR1417 and SLR1565, were purified. The absorption spectrum of purified SLR1565 was typical for [2Fe-2S] cluster-containing proteins, whereas that of SLR1417 predominantly showed the presence of the iron ion alone. In the cyanobacterial cell extracts, only SLR1565 was found to form a complex with a novel prokaryotic HEAT-repeats-containing protein, SLR1098. Thus, the two cyanobacterial IscA protein homologs exist in distinct molecular states, suggesting different cellular roles for these proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Azotobacter vinelandii
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Chromatography, Gel
  • Cyanobacteria
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism
  • Macromolecular Substances
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Binding
  • Repetitive Sequences, Amino Acid
  • Sequence Homology, Amino Acid
  • Spectrum Analysis
  • Subcellular Fractions / chemistry


  • Bacterial Proteins
  • Carrier Proteins
  • Iron-Sulfur Proteins
  • Macromolecular Substances