PMID- 21594712
OWN - NLM
STAT- MEDLINE
DCOM- 20140707
LR  - 20211020
IS  - 1573-5079 (Electronic)
IS  - 0166-8595 (Linking)
VI  - 111
IP  - 1-2
DP  - 2012 Mar
TI  - Gene sequencing and characterization of the light-harvesting complex 2 from 
      thermophilic purple sulfur bacterium Thermochromatium tepidum.
PG  - 9-18
LID - 10.1007/s11120-011-9658-9 [doi]
AB  - In this study, gene sequences coding for the light-harvesting (LH) 2 polypeptides 
      from a thermophilic purple sulfur bacterium Thermochromatium tepidum are reported 
      and characterization of the LH2 complex is described. Three sets of pucBA genes 
      have been identified, and the gene products have been analyzed by electrophoresis 
      and reversed-phase chromatography. The result shows that all of the genes are 
      expressed but the distribution of the expression is not uniform. The gene 
      products undergo post-translational modification, where two of the beta-polypeptides 
      appear to be N-terminally methylated. Absorption spectrum of the purified LH2 
      complex exhibits Q (y) transitions at 800 and 854 nm in dodecyl beta-maltopyranoside 
      solution, and the circular dichroism spectrum shows a "molischianum"-like 
      characteristic. No spectral change was observed for the LH2 when the bacterium 
      was cultured under different conditions of light intensity. In lauryl 
      dimethylamine N-oxide (LDAO) solution, significant changes in the absorption 
      spectrum were observed. The B850 peak decreased and blue-shifted with increasing 
      the LDAO concentration, whereas the B800 intensity increased without change in 
      the peak position. The spectral changes can be partially or almost completely 
      reversed by addition of metal ions, and the divalent cations seem to be more 
      effective. The results indicate that ionic interactions may exist between LH2, 
      detergent molecules and metal ions. Possible mechanisms involved in the 
      detergent- and cation-induced spectral changes are discussed.
FAU - Sekine, Fumie
AU  - Sekine F
AD  - Faculty of Science, Ibaraki University, Mito, 310-8512, Japan.
FAU - Horiguchi, Kentaro
AU  - Horiguchi K
FAU - Kashino, Yasuhiro
AU  - Kashino Y
FAU - Shimizu, Yuuki
AU  - Shimizu Y
FAU - Yu, Long-Jiang
AU  - Yu LJ
FAU - Kobayashi, Masayuki
AU  - Kobayashi M
FAU - Wang, Zheng-Yu
AU  - Wang ZY
LA  - eng
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PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110519
PL  - Netherlands
TA  - Photosynth Res
JT  - Photosynthesis research
JID - 100954728
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA, Bacterial)
RN  - 0 (Light-Harvesting Protein Complexes)
RN  - 0 (Peptides)
RN  - 70FD1KFU70 (Sulfur)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/genetics/isolation & purification/metabolism
MH  - Base Sequence
MH  - Chromatiaceae/genetics/*metabolism
MH  - Chromatography, Reverse-Phase
MH  - DNA, Bacterial/chemistry/genetics
MH  - Gene Expression Regulation, Bacterial
MH  - Light-Harvesting Protein Complexes/*genetics/isolation & purification/*metabolism
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Peptides/genetics/isolation & purification/metabolism
MH  - Protein Processing, Post-Translational
MH  - Sequence Analysis, DNA
MH  - Sulfur/metabolism
EDAT- 2011/05/20 06:00
MHDA- 2014/07/08 06:00
CRDT- 2011/05/20 06:00
PHST- 2010/11/25 00:00 [received]
PHST- 2011/04/18 00:00 [accepted]
PHST- 2011/05/20 06:00 [entrez]
PHST- 2011/05/20 06:00 [pubmed]
PHST- 2014/07/08 06:00 [medline]
AID - 10.1007/s11120-011-9658-9 [doi]
PST - ppublish
SO  - Photosynth Res. 2012 Mar;111(1-2):9-18. doi: 10.1007/s11120-011-9658-9. Epub 2011 
      May 19.