The Slr0924 protein of Synechocystis sp strain PCC 6803 resembles a subunit of the chloroplast protein import complex and is mainly localized in the thylakoid lumen

被引:16
作者
Fulda, S
Norling, B
Schoor, A
Hagemann, M
机构
[1] Univ Rostock, Fachbereich Biowissensch, Inst Mol Physiol & Biotechnol, D-18051 Rostock, Germany
[2] Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs Nat Sci, S-10691 Stockholm, Sweden
[3] Ernst Moritz Arndt Univ Greifswald, D-17487 Greifswald, Germany
关键词
cyanobacteria; protein import; Synechocystis sp strain PCC 6803; thylakoids;
D O I
10.1023/A:1014472322835
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
An isolated 25 kDa protein of Synechocystis sp. PCC 6803 was N-terminally sequenced and assigned to a protein encoded by the ORF slr0924. This ORF shows a certain degree of sequence similarity to a subunit from the protein Translocon at the Inner envelope of pea Chloroplasts (Tic22). The deduced amino acid sequence of Slr0924 has a N-terminal extension, that contains two possible translational start points and two possible cleavage sites for leader peptidases. Immunostaining with an antibody raised to the over-produced protein revealed two cross-reacting forms, which probably correspond to a larger intermediate and the mature protein. Immunogold labelling of thin sections showed that the protein is located mainly in the thylakoid region. This result was verified by thylakoid membrane fractionation indicating that Slr0924 is a lumenal protein. The slr0924 gene product is essential for the viability of Synechocystis sp. PCC 6803 as shown by interposon mutagenesis. The merodiploid strain showed reduced photosynthetic activity compared to the wild-type, Furthermore, growth of the merodiploid strain was found to be completely inhibited after cultivation with glucose. Accordingly, the amount of the slr0924 gene product was regulated by glucose and light intensities in wild-type cells. The potential function of the protein in Synechocystis sp. PCC 6803 will be discussed.
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页码:107 / 118
页数:12
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