REASSEMBLY OF SYNECHOCYSTIS SP PCC-6803 F1-ATPASE FROM ITS OVER-EXPRESSED SUBUNITS

Autor(en): STEINEMANN, D
ENGELBRECHT, S
LILL, H
Stichwörter: ATPASE; BETA-SUBUNIT; BINDING; Biochemistry & Molecular Biology; Biophysics; Cell Biology; CHLOROPLAST ATP SYNTHASE; COMPLEX; DELTA; EXPRESSION; F0F1; F1; PURIFICATION; SYNECHOCYSTIS; THYLAKOIDS
Erscheinungsdatum: 1995
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEBS LETTERS
Volumen: 362
Ausgabe: 2
Startseite: 171
Seitenende: 174
Zusammenfassung: 
Subunits alpha, beta, and gamma of the F-1-part of cyanobacterial F0F1-ATPase have been cloned into expression vectors, Overexpressed subunit beta was found soluble in the cytoplasmic fraction of Escherichia coli cells under appropriate culture and induction conditions and was purified from cell extracts, Recombinant alpha and gamma subunits precipitated into inclusion bodies and had to be solubilized, purified and refolded, The correct folding and functional integrity of the alpha and beta subunits was monitored by their ability to bind nucleotides. Active cyanobacterial F-1-ATPase was assembled from its purified subunits alpha, beta, gamma, delta and epsilon, The reassembled enzyme reconstituted ATP synthesis in F-1-depleted thylakoid membranes of Synechocystis sp, PCC 6803 and hydrolyzed ATP.
ISSN: 00145793
DOI: 10.1016/0014-5793(95)00238-5

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