Chlorosome proteins studied by MALDI-TOF-MS: topology of CsmA in Chlorobium tepidum.

Abstract:

:Chlorosomes, the light-harvesting apparatus of green bacteria, are a unique antenna system, in which pigments are organized in aggregates rather than associated with proteins. Isolated chlorosomes from the green sulphur bacterium Chlorobium tepidum contain 10 surface-exposed proteins. Treatment of chlorosomes from Chlorobium tepidum with protease caused changes in the spectral properties of bacteriochlorophyll c and digestion of chlorosome proteins. Using SDS-PAGE analysis, immunoblotting and matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) we have investigated the topology of the 59-residue CsmA protein. Our results show that at the N-terminus, the only amino acid available for protease degradation is the methionine. At the C-terminus, amino acids can be removed by protease treatment to produce a residual protein containing at least the sequence between residues 2 and 38. These results indicate that the N-terminal portion of the CsmA protein, which is predicted to be mainly hydrophobic, is buried in the chlorosome envelope.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Milks KJ,Danielsen M,Persson S,Jensen ON,Cox RP,Miller M

doi

10.1007/s11120-005-3757-4

subject

Has Abstract

pub_date

2005-11-01 00:00:00

pages

113-21

issue

1-2

eissn

0166-8595

issn

1573-5079

journal_volume

86

pub_type

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