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J. Biol. Chem., Vol. 277, Issue 14, 12446-12455, April 5, 2002

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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

From  UMR 7099, CNRS and Université Paris-7, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, Paris F-75005, France, ^¶ UMR 7637, Ecole Supérieure de Physique et Chimie Industrielles de la Ville de Paris, 10 rue Vauquelin, Paris F-75005, France, and  Centro di Studio del C.N.R. sulla Biologia Cellulare e Molecolare delle Piante, Università degli Studi di Milano, via Celoria 26, Milano 20133, Italy, and UPR 1261, CNRS, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, Paris F-75005, France

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 led to the following conclusions: (i) neither a free subunit IV C terminus nor a free PetL N terminus is required for assembly of the b₆f complex; (ii) the first AUG codon in the sequence of the 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 b₆f complex from C. reinhardtii contains an eighth, hitherto unrecognized subunit, PetN; and (vi) the ability to perform state transitions is lost in the chimeric mutants, although (vii) the Q-cycle is unaffected. A structural hypothesis is presented to account for this peculiar phenotype.

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