Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus

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Standard

Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus. / Sakuragi, Y; Frigaard, N-U; Shimada, K; Matsuura, K.

In: BBA General Subjects, Vol. 1413, No. 3, 1999, p. 172-180.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sakuragi, Y, Frigaard, N-U, Shimada, K & Matsuura, K 1999, 'Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus', BBA General Subjects, vol. 1413, no. 3, pp. 172-180. https://doi.org/10.1016/S0005-2728(99)00092-4

APA

Sakuragi, Y., Frigaard, N-U., Shimada, K., & Matsuura, K. (1999). Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus. BBA General Subjects, 1413(3), 172-180. https://doi.org/10.1016/S0005-2728(99)00092-4

Vancouver

Sakuragi Y, Frigaard N-U, Shimada K, Matsuura K. Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus. BBA General Subjects. 1999;1413(3):172-180. https://doi.org/10.1016/S0005-2728(99)00092-4

Author

Sakuragi, Y ; Frigaard, N-U ; Shimada, K ; Matsuura, K. / Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus. In: BBA General Subjects. 1999 ; Vol. 1413, No. 3. pp. 172-180.

Bibtex

@article{8dbe34b0962611de8bc9000ea68e967b,
title = "Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus",
abstract = "The protein assumed to be associated with bacteriochlorophyll (BChl) a in chlorosomes from the photosynthetic green filamentous bacterium Chloroflexus aurantiacus was investigated by alkaline treatment, proteolytic digestion and a new treatment using 1-hexanol, sodium cholate and Triton X-100. Upon alkaline treatment, only the 5.7 kDa CsmA protein was removed from the chlorosomes among six proteins detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis, concomitantly with the disappearance of BChl a absorption at 795 nm. Trypsin treatment removed two proteins with molecular masses of 11 and 18 kDa (CsmN and CmsM), whereas the spectral properties of BChl a and BChl c were not changed. By the new hexanol-detergent (HD) treatment, most BChl c and all of the detected proteins except CsmA were removed from the chlorosomes without changing the BChl a spectral properties. Subsequent proteinase K treatment of these HD-treated chlorosomes caused digestion of CsmA and a simultaneous decrease of the BChl a absorption band. Based on these results, we suggest that CsmA is associated with BChl a in the chlorosomes. This suggestion was supported by the measured stoichiometric ratio of BChl a to CsmA in isolated chlorosomes, which was estimated to be between 1.2 and 2.7 by amino acid analysis of the SDS-PAGE-resolved protein bands.",
author = "Y Sakuragi and N-U Frigaard and K Shimada and K Matsuura",
note = "Keywords: Amino Acids; Bacterial Proteins; Bacteriochlorophylls; Chlorates; Chlorobi; Electrophoresis, Polyacrylamide Gel; Hexanols; Octoxynol; Sodium Hydroxide; Subcellular Fractions; Trypsin",
year = "1999",
doi = "10.1016/S0005-2728(99)00092-4",
language = "English",
volume = "1413",
pages = "172--180",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus

AU - Sakuragi, Y

AU - Frigaard, N-U

AU - Shimada, K

AU - Matsuura, K

N1 - Keywords: Amino Acids; Bacterial Proteins; Bacteriochlorophylls; Chlorates; Chlorobi; Electrophoresis, Polyacrylamide Gel; Hexanols; Octoxynol; Sodium Hydroxide; Subcellular Fractions; Trypsin

PY - 1999

Y1 - 1999

N2 - The protein assumed to be associated with bacteriochlorophyll (BChl) a in chlorosomes from the photosynthetic green filamentous bacterium Chloroflexus aurantiacus was investigated by alkaline treatment, proteolytic digestion and a new treatment using 1-hexanol, sodium cholate and Triton X-100. Upon alkaline treatment, only the 5.7 kDa CsmA protein was removed from the chlorosomes among six proteins detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis, concomitantly with the disappearance of BChl a absorption at 795 nm. Trypsin treatment removed two proteins with molecular masses of 11 and 18 kDa (CsmN and CmsM), whereas the spectral properties of BChl a and BChl c were not changed. By the new hexanol-detergent (HD) treatment, most BChl c and all of the detected proteins except CsmA were removed from the chlorosomes without changing the BChl a spectral properties. Subsequent proteinase K treatment of these HD-treated chlorosomes caused digestion of CsmA and a simultaneous decrease of the BChl a absorption band. Based on these results, we suggest that CsmA is associated with BChl a in the chlorosomes. This suggestion was supported by the measured stoichiometric ratio of BChl a to CsmA in isolated chlorosomes, which was estimated to be between 1.2 and 2.7 by amino acid analysis of the SDS-PAGE-resolved protein bands.

AB - The protein assumed to be associated with bacteriochlorophyll (BChl) a in chlorosomes from the photosynthetic green filamentous bacterium Chloroflexus aurantiacus was investigated by alkaline treatment, proteolytic digestion and a new treatment using 1-hexanol, sodium cholate and Triton X-100. Upon alkaline treatment, only the 5.7 kDa CsmA protein was removed from the chlorosomes among six proteins detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis, concomitantly with the disappearance of BChl a absorption at 795 nm. Trypsin treatment removed two proteins with molecular masses of 11 and 18 kDa (CsmN and CmsM), whereas the spectral properties of BChl a and BChl c were not changed. By the new hexanol-detergent (HD) treatment, most BChl c and all of the detected proteins except CsmA were removed from the chlorosomes without changing the BChl a spectral properties. Subsequent proteinase K treatment of these HD-treated chlorosomes caused digestion of CsmA and a simultaneous decrease of the BChl a absorption band. Based on these results, we suggest that CsmA is associated with BChl a in the chlorosomes. This suggestion was supported by the measured stoichiometric ratio of BChl a to CsmA in isolated chlorosomes, which was estimated to be between 1.2 and 2.7 by amino acid analysis of the SDS-PAGE-resolved protein bands.

U2 - 10.1016/S0005-2728(99)00092-4

DO - 10.1016/S0005-2728(99)00092-4

M3 - Journal article

C2 - 10556629

VL - 1413

SP - 172

EP - 180

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 3

ER -

ID: 14095798