Preliminary Studies on the Operon Coding for the Reaction Center Polypeptides in Chloroflexus Aurantiacus

  • Judith A. Shiozawa
  • Katalin Csiszȧr
  • Reiner Feick
Part of the FEMS Symposium book series (FEMSS)


The isolated reaction center of the thermophilic, facultative photoheterotroph Chloroflexus (C.) aurantiacus is composed of two polypeptides (Shiozawa et al., 1987). The genes encoding the two polypeptides have been cloned and sequenced (Shiozawa et al., 1989 and Ovchinnikov et al., 1988 a, b). The two genes are adjacent to one another; 17 bases separate the stop codon of the L-gene and the start codon of the M-gene. The deduced amino acid sequences are about 40% similar to the respective subunits of Rhodobacter sphaeroides. We have now undertaken studies to determine if the puf operon of this green nonsulfur bacteria is similar to that of Rhodospirillaceae.


Rhodobacter Sphaeroides Putative Promoter Sequence Primer Extension Experiment Poten Tial Open Reading Frame CHLOROFLEXUS AURANTIACUS 
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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Judith A. Shiozawa
    • 1
  • Katalin Csiszȧr
    • 1
  • Reiner Feick
    • 1
  1. 1.Max-Planck Institut für BiochemieMartinsried b. MünchenDeutschland

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