Phylogenomic analysis of energy converting enzymes

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dc.contributor.advisorPD Dr. Armen Mulkidjanian
dc.creatorDibrova, Daria
dc.date.accessioned2013-06-12T07:32:06Z
dc.date.available2013-06-12T07:32:06Z
dc.date.issued2013-06-12T07:32:06Z
dc.identifier.urihttps://repositorium.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2013061210923-
dc.description.abstractIn this thesis, phylogenomic and comparative structural analyses of several widespread energy converting enzymes were performed. The focus was on the major subfamilies of the enzymes that process nucleoside triphosphates (ATP and GTP) and on some key enzymes of the electron transfer chains. First, we analyzed the P-loop GTPases, RadA/RecA recombinases, chaperone GroEL, branched-chain α-ketoacid dehydrogenase kinases, chaperone Hsc70, actins, and membrane pyrophosphatases. In the each inspected family we could identify (1) members which were potassium-dependent and/or contained K+ ions in the active site, and (2) potassium-independent enzymes with lysine or arginine residues as catalytic groups that occupy the positions of potassium ions in the homologous, K+-dependent enzymes. Based on the results of our analyses, we suggest that the appearance of the K+-binding sites could precede in evolution the recruitment of positively charged residues (lysine or arginine "fingers") with the latter providing more possibilities to control the enzyme reactions. Second, we have described the distinctive features of a phylogenetically separated subfamily of rotary membrane ATPases which we named N-ATPases. The N-ATPases have a specific operon organization with two additional subunits, absent in other rotary ATPases, and a complete set of Na+-binding ligands in the membrane c-subunits. We made a prediction, which was later confirmed, that these enzymes are capable of Na+ translocation across the membrane and may confer salt tolerance on marine prokaryotes. Third, phylogenomic analysis of the cytochrome bc complexes suggests that these enzyme complexes initially emerged within the bacteria and were then transferred to archaea via lateral gene transfer on several independent occasions. Our analysis indicates that the ancestral form of the cytochrome bc complex was a b6f-type complex; the fusion of the cytochrome b6 and the subunit IV to a "long" cytochrome b of the cytochrome bc1 complexes could have happened in different lineages independently. Fourth, our phylogenomic and comparative structural analyses of the cytochrome bc1 complex and of cytochrome c allowed us to trace how these enzymes became involved in triggering of apoptosis in Metazoa. We could trace the emergence of a specific cardiolipin-binding site within the cytochrome bc complex and the evolution of structural traits that account for the involvement of the cytochrome c as a trigger of apoptosis in vertebrates.eng
dc.rightsNamensnennung - Nicht-kommerziell - Weitergabe unter gleichen Bedingungen 3.0 Unported-
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/-
dc.subjectbioenergeticseng
dc.subjectkinaseeng
dc.subjectGTPaseeng
dc.subjectmolecular evolutioneng
dc.subjectbioinformaticseng
dc.subjectabiogenesiseng
dc.subjectrespirationeng
dc.subjectphotosynthesiseng
dc.subjectsodium-potassium gradienteng
dc.subjectproton transporteng
dc.subjectlast universal ancestoreng
dc.subjectphylogenomic analysiseng
dc.subjectATPaseeng
dc.subjectATPeng
dc.subjectbiological membraneseng
dc.subjectApaf-1eng
dc.subjectcytochrome ceng
dc.subjectapoptosiseng
dc.subjectATP synthaseeng
dc.subjectcomplex IIIeng
dc.subject.ddc570 - Biowissenschaften; Biologie
dc.titlePhylogenomic analysis of energy converting enzymeseng
dc.title.alternativePhylogenomische Analyse energieumwandelnder Enzymeger
dc.title.alternativeФилогеномный анализ энергопреобразующих ферментовrus
dc.typeDissertation oder Habilitation [doctoralThesis]-
thesis.locationOsnabrück-
thesis.institutionUniversität-
thesis.typeDissertation [thesis.doctoral]-
thesis.date2013-05-29-
dc.contributor.refereeJun.-Prof. Dr. Karin Busch
dc.subject.bk42.10 - Theoretische Biologie
vCard.ORGFB5
Appears in Collections:FB05 - E-Dissertationen

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