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Papers In Press, published online ahead of print January 16, 2002
J. Biol. Chem, 10.1074/jbc.M110914200
Submitted on November 14, 2001
Revised on January 16, 2002
Accepted on January 15, 2002

Chimeric fusions of subunit IV and PetL in the b6f complex of Chlamydomonas reinhardtii : structural implications and consequences on State Transitions

Francesca Zito, Joëlle Vinh, Jean-Luc Popot, and Giovanni Finazzi

CNRS UMR7099, Institut de Biologie Physico Chimique, Paris 75005

Corresponding Author: zito{at}ibpc.fr

The cytochrome b6f complex of Chlamydomonas reinhardtii contains four large subunits and at least three small ones, PetG, PetL and PetM, whose role and location are unknown. Chimeric proteins have been constructed, in which the C-terminus of subunit IV is fused to either one or the other of the two putative N-termini of PetL. Biochemical and functional analysis of the chimeras together with mass spectrometry analysis of the wild-type (WT) complex lead to the following conclusions : i) neither a free subunit IV C-terminus nor a free PetL N-terminus is required for assembly of the b6 f complex ; ii) the first AUG codon in the sequence of gene petL is used for initiation ; iii) the N-terminus of WT PetL lies in the lumen ; iv) in the WT complex, the N-terminus of PetL and the C-terminus of subunit IV are within reach of each other ; v) the purified b6 f complex from C. reinhardtii contains an eight, hitherto unrecognized subunit, PetN ; vi) the ability to perform State Transitions is lost in the chimeric mutants, even though vii) the Q-cycle is unaffected. A structural hypothesis is presented to account for this peculiar phenotype.


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