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Kupriyanova, E. V.,Cho, S. M.,Park, Y. I.,Pronina, N. A.,Los, D. A. Springer Science + Business Media 2016 Photosynthesis research Vol.130 No.1
<P>At present geological epoch, the carbon concentrating mechanism (CCM) of cyanobacteria represents the obligatory tool for adaptation to low content of CO2 in the atmosphere and for the maintenance of sufficient photosynthetic activity. Functional CCM was found in modern cyanobacteria from different ecological niches. However, the presence of such mechanism in species that inhabit soda lakes is not obvious due to high content of inorganic carbon (C (i)) in the environment. Here we analyze CCM components that have been identified by sequencing of the whole genome of the alkaliphilic cyanobacterium Microcoleus sp. IPPAS B-353. The composition of the CCM components of Microcoleus is similar to that of 'model' beta-cyanobacteria, freshwater and marine Synechococcus or Synechocystis spp. However, CahB1 protein of Microcoleus, which is the homolog of CcaA, the carboxysomal beta-type carbonic anhydrase (CA) of beta-cyanobacteria, appeared to be the only active CA located in cell envelopes. The conservative regions of CcmM, CahG (a homolog of archeal gamma-CAs, Cam/CamH), and ChpX of Microcoleus possess single amino acid substitutions that may cause a lack of CA activities. Unlike model cyanobacteria, Microcoleus induces only one BicA-type bicarbonate transporter in response to C (i) limitation. The differences in the appearance of CCM components and in their characteristics between alkaliphilic Microcoleus and freshwater or marine cyanobacteria are described. The possible reasons for the maintenance of CCM components in cyanobacteria, which permanently live at high concentrations of C (i) in soda lakes, are discussed.</P>
Cho, Sung Mi,Jeoung, Sae Chae,Song, Ji-Young,Kupriyanova, Elena V.,Pronina, Natalia A.,Lee, Bong-Woo,Jo, Seong-Whan,Park, Beom-Seok,Choi, Sang-Bong,Song, Ji-Joon,Park, Youn-Il American Society for Biochemistry and Molecular Bi 2015 The Journal of biological chemistry Vol.290 No.47
<P>Cyanobacteriochromes (CBCRs), which are exclusive to and widespread among cyanobacteria, are photoproteins that sense the entire range of near-UV and visible light. CBCRs are related to the red/far-red phytochromes that utilize linear tetrapyrrole (bilin) chromophores. Best characterized from the unicellular cyanobacterium <I>Synechocystis</I> sp. PCC 6803 and the multicellular heterocyst forming filamentous cyanobacteria <I>Nostoc punctiforme</I> ATCC 29133 and <I>Anabaena</I> sp. PCC 7120, CBCRs have been poorly investigated in mat-forming, nonheterocystous cyanobacteria. In this study, we sequenced the genome of one of such species, <I>Microcoleus</I> IPPAS B353 (<I>Microcoleus</I> B353), and identified two phytochromes and seven CBCRs with one or more bilin-binding c<U>G</U>MP-specific phosphodiesterase, <U>a</U>denylyl cyclase and <U>F</U>hlA (GAF) domains. Biochemical and spectroscopic measurements of 23 purified GAF proteins from phycocyanobilin (PCB) producing recombinant <I>Escherichia coli</I> indicated that 13 of these proteins formed near-UV and visible light-absorbing covalent adducts: 10 GAFs contained PCB chromophores, whereas three contained the PCB isomer, phycoviolobilin (PVB). Furthermore, the complement of <I>Microcoleus</I> B353 CBCRs is enriched in near-UV and violet sensors, but lacks red/green and green/red CBCRs that are widely distributed in other cyanobacteria. We hypothesize that enrichment in short wavelength-absorbing CBCRs is critical for acclimation to high-light environments where this organism is found.</P>