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Isolation and characterization of cDNA clones encoding the 17.9 and 8.1 kDa subunits of Photosystem I from Chlamydomonas reinhardtii
Author(s) -
Lars-Gunnar Franz�n,
Gerhard Frank,
H. Zuber,
JeanDavid Rochaix
Publication year - 1989
Publication title -
plant molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.448
H-Index - 174
eISSN - 1573-5028
pISSN - 0167-4412
DOI - 10.1007/bf00017585
Subject(s) - chlamydomonas reinhardtii , biology , complementary dna , thylakoid , peptide sequence , transit peptide , amino acid , nucleic acid sequence , microbiology and biotechnology , photosystem i , biochemistry , southern blot , northern blot , chlamydomonas , gene , photosystem ii , chloroplast , plastid , mutant , photosynthesis
cDNA clones encoding two Photosystem I subunits of Chlamydomonas reinhardtii with apparent molecular masses of 18 and 11 kDa (thylakoid polypeptides 21 and 30; P21 and P30 respectively) were isolated using oligonucleotides, the sequences of which were deduced from the N-terminal amino acid sequences of the proteins. The cDNAs were sequenced and used to probe Southern and Northern blots. The Southern blot analysis indicates that both proteins are encoded by single-copy genes. The mRNA sizes of the two components are 1400 and 740 nucleotides, respectively. Comparison between the open reading frames of the cDNAs and the N-terminal amino acid sequences of the proteins indicates that the molecular masses of the mature proteins are 17.9 (P21) and 8.1 kDa (P30). Analysis of the deduced protein sequences predicts that both subunits are extrinsic membrane proteins with net positive charges. The amino acid sequences of the transit peptides suggest that P21 and P30 are routed towards the lumenal and stromal sides of the thylakoid membranes, respectively.

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