Responses of the Rhodobacter sphaeroides transcriptome to blue light under semiaerobic conditions

被引:53
作者
Braatsch, S
Moskvin, OV
Klug, G
Gomelsky, M
机构
[1] Univ Wyoming, Dept Mol Biol, Dept 3944, Laramie, WY 82071 USA
[2] Univ Giessen, Inst Mikrobiol & Mol Biol, Giessen, Germany
关键词
D O I
10.1128/JB.186.22.7726-7735.2004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Exposure to blue light of the facultative phototrophic proteobacterium Rhodobacter sphaeroides grown semiaerobically results in repression of the puc and puf operons involved in photosystem formation. To reveal the genome-wide effects of blue light on gene expression and the underlying photosensory mechanisms, transcriptome profiles of R. sphaeroides during blue-light irradiation (for 5 to 135 min) were analyzed. Expression of most photosystem genes was repressed upon irradiation. Downregulation of photosystem development may be used to prevent photooxidative damage occurring when the photosystem, oxygen, and high-intensity light are present simultaneously. The photoreceptor of the BLUF-domain family, AppA, which belongs to the AppA-PpsR antirepressor-repressor system, is essential for maintenance of repression upon prolonged irradiation (S. Braatsch et al., Mol. Microbiol. 45:827-836, 2002). Transcriptome data suggest that the onset of repression is also mediated by the AppA-PpsR system, albeit via an apparently different sensory mechanism. Expression of several genes, whose products may participate in photooxidative damage defense, including deoxypyrimidine photolyase, glutathione peroxidase, and quinol oxidoreductases, was increased. Among the genes upregulated were genes encoding two sigma factors: sigma(E) and sigma(38). The consensus promoter sequences for these sigma factors were predicted in the upstream sequences of numerous upregulated genes, suggesting that coordinated action of sigma(E) and sigma(38) is responsible for the upregulation. Based on the dynamics of upregulation, the anti-sigma(E) factor ChrR or its putative upstream partner is proposed to be the primary sensor. The identified transcriptome responses provided a framework for deciphering blue-light-dependent signal transduction pathways in R. sphaeroides.
引用
收藏
页码:7726 / 7735
页数:10
相关论文
共 68 条
[1]   HY4 GENE OF A-THALIANA ENCODES A PROTEIN WITH CHARACTERISTICS OF A BLUE-LIGHT PHOTORECEPTOR [J].
AHMAD, M ;
CASHMORE, AR .
NATURE, 1993, 366 (6451) :162-166
[2]   New family of regulators in the environmental signaling pathway which activates the general stress transcription factor σB of Bacillus subtilis [J].
Akbar, S ;
Gaidenko, TA ;
Kang, CM ;
O'Reilly, M ;
Devine, KM ;
Price, CW .
JOURNAL OF BACTERIOLOGY, 2001, 183 (04) :1329-1338
[3]   COMPLETE CHEMICAL-STRUCTURE OF PHOTOACTIVE YELLOW PROTEIN - NOVEL THIOESTER-LINKED 4-HYDROXYCINNAMYL CHROMOPHORE AND PHOTOCYCLE CHEMIST [J].
BACA, M ;
BORGSTAHL, GEO ;
BOISSINOT, M ;
BURKE, PM ;
WILLIAMS, DR ;
SLATER, KA ;
GETZOFF, ED .
BIOCHEMISTRY, 1994, 33 (48) :14369-14377
[4]   Mechanisms for redox control of gene expression [J].
Bauer, CE ;
Elsen, S ;
Bird, TH .
ANNUAL REVIEW OF MICROBIOLOGY, 1999, 53 :495-523
[5]   Rapid blue light regulation of a Trichoderma harzianum photolyase gene [J].
Berrocal-Tito, G ;
Sametz-Baron, L ;
Eichenberg, K ;
Horwitz, BA ;
Herrera-Estrella, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (20) :14288-14294
[6]   ORF90, a gene required for photoreactivation in Rhodobacter capsulatus SB1003 encodes a cyclobutane pyrimidine dimer photolyase [J].
Braatsch, S ;
Klug, G .
PHOTOSYNTHESIS RESEARCH, 2004, 79 (02) :167-177
[7]   Blue light perception in bacteria [J].
Braatsch, S ;
Klug, G .
PHOTOSYNTHESIS RESEARCH, 2004, 79 (01) :45-57
[8]   A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides [J].
Braatsch, S ;
Gomelsky, M ;
Kuphal, S ;
Klug, G .
MOLECULAR MICROBIOLOGY, 2002, 45 (03) :827-836
[9]   Identification of a new cryptochrome class: Structure, function, and evolution [J].
Brudler, R ;
Hitomi, K ;
Daiyasu, H ;
Toh, H ;
Kucho, K ;
Ishiura, M ;
Kanehisa, M ;
Roberts, VA ;
Todo, T ;
Tainer, JA ;
Getzoff, ED .
MOLECULAR CELL, 2003, 11 (01) :59-67
[10]   Dissection of the triple tryptophan electron transfer chain in Escherichial coli DNA photolyase:: Trp382 is the primary donor in photoactivation [J].
Byrdin, M ;
Eker, APM ;
Vos, MH ;
Brettel, K .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (15) :8676-8681