Spectral characteristic of fluorescence induction in a model cyanobacterium, Synechococcus sp. (PCC 7942).

نویسندگان

  • Radek Kana
  • Ondrej Prásil
  • Ondrej Komárek
  • George C Papageorgiou
  • Govindjee
چکیده

We present here three-dimensional time-wavelength-intensity displays of changes in variable fluorescence, during the O(JI)PSMT transient, observed in cyanobacterium at room temperature. We were able to measure contributions of individual chromophores to fluorescence spectra at various times of fluorescence induction (FI). The method was applied to a freshwater cyanobacterium, Synechococcus sp. (PCC 7942). Analysis of our experimental results provides the following new conclusions: (i) the main chlorophyll (Chl) a emission band at approximately 685 nm that originates in Photosystem (PS) II exhibits typical fast (OPS) and slow (SMT) FI kinetics with both orange (622 nm) and blue (464 nm) excitation. (ii) Similar kinetics are exhibited for its far-red emission satellite band centered at approximately 745 nm, where the PS II contribution predominates. (iii) A significant OPS-SMT-type kinetics of C-phycocyanin emission at approximately 650 nm are observed with the blue light excitation, but not with orange light excitation where the signal rose only slightly to a maximum. The induction of F650 was not caused by an admixture of the F685 fluorescence and thus our data show light-inducible and dark-reversible changes of phycobilin fluorescence in vivo. We discuss possible interpretations of this new observation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Spectroscopic properties of PSI-IsiA supercomplexes from the cyanobacterium Synechococcus PCC 7942.

The cyanobacterium Synechococcus PCC 7942 grown under iron starvation assembles a supercomplex consisting of a trimeric Photosystem I (PSI) complex encircled by a ring of 18 CP43' or IsiA light-harvesting complexes [Nature 412 (2001) 745]. Here we present a spectroscopic characterization by temperature-dependent absorption and fluorescence spectroscopy, site-selective fluorescence spectroscopy ...

متن کامل

Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.

The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 signals the cellular state of nitrogen assimilation relative to CO2 fixation by being phosphorylated at a seryl residue. In this study, we first determined the location of the phosphorylated seryl residue within the PII amino acid sequence. The phosphorylation site exhibits an RXS motif, a recognition sequence characteristi...

متن کامل

Promoters of the phycocyanin gene clusters of the cyanobacterium Synechococcus sp. strain PCC 7942.

The cyanobacterium Synechococcus sp. strain PCC 7942 has duplicated phycocyanin subunit gene clusters cpcB1A1 and cpcB2A2, which are identical to each other and to those of Synechococcus sp. strain PCC 6301 (Anacystis nidulans). Nucleotide sequences of the 428 and 286 bases of the 5' non-coding regions of the cpcB1A1 and cpcB2A2 clusters, respectively, of strain PCC 7942 were identical to those...

متن کامل

Expression of Escherichia coli phosphoenolpyruvate carboxylase in a cyanobacterium. Functional complementation of Synechococcus PCC 7942 ppc.

The gene (ppc) coding for phosphoenolpyruvate carboxylase (PEPCase) in the cyanobacterium Synechococcus PCC 7942 has been inactivated via insertional mutagenesis while being functionally complemented by Escherichia coli ppc. Cyanobacterial cells functionally complemented by E. coli ppc showed decreased PEPCase activity in crude cell lysates and detergent-permeabilized whole cell assays. Decreas...

متن کامل

Protection of psbAII transcript from ribonuclease degradation in vitro by DnaK2 and DnaJ2 chaperones of the cyanobacterium Synechococcus elongatus PCC 7942.

Three dnaK and four dnaJ genes have been identified in the genome of cyanobacterium Synechococcus elongatus PCC 7942. Our comprehensive analysis of yeast two-hybrid screening revealed a specific interaction among DnaK2, DnaJ2, and RNase E, an essential endoribonuclease. We examined the effects of DnaK2 and DnaJ2 on RNase E activity by monitoring the digestion of psbAII transcript in vitro. The ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochimica et biophysica acta

دوره 1787 10  شماره 

صفحات  -

تاریخ انتشار 2009