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Volume 271, Number 51, Issue of December 20, 1996 pp. 32737-32742
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Cross-linking of Engineered Subunit delta  to (alpha beta )3 in Chloroplast F-ATPase

(Received for publication, May 7, 1996, and in revised form, September 10, 1996)

Holger Lill , Frank Hensel , Wolfgang Junge and Siegfried Engelbrecht

From Biophysik, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastrasse 11, D-49069 Osnabrück, Federal Republic of Germany

Ser right-arrow Cys mutations were introduced into subunit delta  of spinach chloroplast F0F1-ATPase (CF0CF1) by site-directed mutagenesis. The engineered delta  subunits were overexpressed in Escherichia coli, purified, and reassembled with spinach chloroplast F1-ATPase (CF1) lacking the delta  subunit (CF1(-delta )). By modification with eosin-5-maleimide, it was shown that residues 10, 57, 82, 160, and 166 were solvent-accessible in isolated CF1 and all but residue 166 also in membrane-bound CF0CF1. Modification of the engineered delta  subunit with photolabile cross-linkers, binding of delta  to CF1(-delta ), and photolysis yielded the same SDS gel pattern of cross-link products in the presence or absence of ADP, phosphate, and ATP and both in soluble CF1 and in CF0CF1. By chemical hydrolysis of cross-linked CF1, it was shown that delta S10C was cross-linked within the N-terminal 62 residues of subunit beta . delta S57C, delta S82C, and delta S166C were cross-linked within the N-terminal 192 residues of subunit alpha . Cross-linking affected neither ATP hydrolysis by soluble CF1 nor its ability to reassemble with CF0 and to structurally reconstitute ATP synthesis. Functional reconstitution, however, seemed to be impaired.


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