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Journal of Bacteriology, February 2003, p. 1415-1422, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1415-1422.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

ldpA Encodes an Iron-Sulfur Protein Involved in Light-Dependent Modulation of the Circadian Period in the Cyanobacterium Synechococcus elongatus PCC 7942

Mitsunori Katayama,1,2,{dagger} Takao Kondo,2 Jin Xiong,1 and Susan S. Golden1*

Department of Biology, Texas A&M University, College Station, Texas 77843-3258,1 Division of Biological Science, Graduate School of Science, Nagoya University, and CREST, Japan Science and Technology Corporation, Chikusa-ku, Nagoya 464-8602, Japan2

Received 5 August 2002/ Accepted 28 October 2002

We generated random transposon insertion mutants to identify genes involved in light input pathways to the circadian clock of the cyanobacterium Synechococcus elongatus PCC 7942. Two mutants, AMC408-M1 and AMC408-M2, were isolated that responded to a 5-h dark pulse differently from the wild-type strain. The two mutants carried independent transposon insertions in an open reading frame here named ldpA (for light-dependent period). Although the mutants were isolated by a phase shift screening protocol, the actual defect is a conditional alteration in the circadian period. The mutants retain the wild-type ability to phase shift the circadian gene expression (bioluminescent reporter) rhythm if the timing of administration of the dark pulse is corrected for a 1-h shortening of the circadian period in the mutant. Further analysis indicated that the conditional short-period mutant phenotype results from insensitivity to light gradients that normally modulate the circadian period in S. elongatus, lengthening the period at low light intensities. The ldpA gene encodes a polypeptide that predicts a 7Fe-8S cluster-binding motif expected to be involved in redox reactions. We suggest that the LdpA protein modulates the circadian clock as an indirect function of light intensity by sensing changes in cellular physiology.

* Corresponding author. Mailing address: Department of Biology, Texas A&M University, 3258 TAMU, College Station, TX 77843-3258. Phone: (979) 845-9824. Fax: (979) 862-7659. E-mail: sgolden{at}tamu.edu.

{dagger} Present address: University of Tokyo, Meguro, Tokyo 153-8902, Japan.

Journal of Bacteriology, February 2003, p. 1415-1422, Vol. 185, No. 4
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.4.1415-1422.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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