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Cyanobacterial and chloroplast F1-ATPases: cross-reconstitution of photophosphorylation and subunit immunological relationships

dc.contributor.authorHicks, David B.en_US
dc.contributor.authorNelson, Nathanen_US
dc.contributor.authorYocum, Charles F.en_US
dc.date.accessioned2006-04-07T19:26:35Z
dc.date.available2006-04-07T19:26:35Z
dc.date.issued1986-09-10en_US
dc.identifier.citationHicks, David B., Nelson, Nathan, Yocum, Charles F. (1986/09/10)."Cyanobacterial and chloroplast F1-ATPases: cross-reconstitution of photophosphorylation and subunit immunological relationships." Biochimica et Biophysica Acta (BBA) - Bioenergetics 851(2): 217-222. <http://hdl.handle.net/2027.42/26048>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1S-47RS57N-SY/2/0ada4b947bb58544e1e52a961d6f56b7en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/26048
dc.description.abstractThe photosynthetic F1-ATPase from the cyanobacterium Spirulina platensis was recently purified in a five-subunit, reconstitutively active form (Hicks, D.B. and Yocum, C.F. (1986) Arch. Biochem. Biophys. 245, 220-229). Here we report on the similarities of the cyanobacterial F1 to the higher plant chloroplast F1 (CF1), as judged by two distinct methods. The ability of each coupling factor to reconstitute photophosphorylation in photosynthetic membranes depleted of F1 content by 2 M NaBr treatment was tested. Addition of either the homologous enzyme (e.g., Spirulina F1, Spirulina membranes) or the heterologous enzyme (e.g., spinach CF1 Spirulina membranes) to depleted membranes increased the rate of phenazine methosulfate-dependent cyclic photophosphorylation from nearly zero to up to 70 [mu]mol ATP/h per mg Chl. Antibodies against four subunits of CF1 ([alpha], [gamma], [delta] and [var epsilon]) and against [beta] of Escherichia coli F1 were reacted with the Spirulina enzyme by protein blotting. The [alpha], [beta] and [gamma] subunits of Spirulina F1 cross-reacted with antibodies against the corresponding subunits from spinach. The cross-reactivity of the [gamma] subunit correlated with previous observations that Spirulina membrane ATPase activity can be modulated by light and dithiothreitol, in a similar fashion to their effect on the enzyme from spinach chloroplasts. The ability of cyanobacterial and chloroplast enzymes to restore activity to heterologous membranes in the absence of immunological similarities between their respective [delta] and [var epsilon] subunits may suggest that structural features other than particular amino acid sequences of these subunits are paramount in their roles in binding F1 to the membrane and in sealing proton leaks.en_US
dc.format.extent569453 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCyanobacterial and chloroplast F1-ATPases: cross-reconstitution of photophosphorylation and subunit immunological relationshipsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biology, University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biology, University of Michigan, Ann Arbor, MI 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartment of Biochemistry, Roche Institute of Molecular Biology, Nutley, NJ 07110, U.S.A.en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/26048/1/0000121.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2728(86)90128-3en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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