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Disruption and complementation of the selenocysteine biosynthesis pathway reveals a hierarchy of selenoprotein gene expression in the archaeon Methanococcus maripaludis

Titelangaben

Stock, Tilmann ; Selzer, Mirjam ; Connery, Sarah ; Seyhan, Deniz ; Resch, Armin ; Rother, Michael:
Disruption and complementation of the selenocysteine biosynthesis pathway reveals a hierarchy of selenoprotein gene expression in the archaeon Methanococcus maripaludis.
In: Molecular Microbiology. Bd. 82 (2011) Heft 3 . - S. 734-747.
ISSN 1365-2958
DOI: https://doi.org/10.1111/j.1365-2958.2011.07850.x

Abstract

Proteins containing selenocysteine are found inmembers of all three domains of life, Bacteria, Eukaryaand Archaea. A dedicated tRNA (tRNAsec) serves asa scaffold for selenocysteine synthesis. However,sequence and secondary structures differ in tRNAsecfrom the different domains. An Escherichia coli strainlacking the gene for tRNAsec could only be complementedwith the homologue from Methanococcusmaripaludis when a single base in the anticodon loopwas exchanged demonstrating that this base is acrucial determinant for archaeal tRNAsec to function inE. coli. Complementation in trans of M. maripaludisJJ mutants lacking tRNAsec, O-phosphoseryl-tRNAseckinase or O-phosphoseryl-tRNAsec:selenocysteinesynthase with the corresponding genes from M. maripaludisS2 restored the mutant’s ability to synthesizeselenoproteins. However, only partial restoration ofthe wild-type selenoproteome was observed as onlyselenocysteine-containing formate dehydrogenasewas synthesized. Quantification of transcripts showedthat disrupting the pathway of selenocysteine synthesisleads to downregulation of selenoprotein geneexpression, concomitant with upregulation of aselenium-independent backup system, which is notre-adjusted upon complementation. This transcriptionalarrest was independent of selenophosphate butdepended on the ‘history’ of the mutants and was inheritable, which suggests that a stable geneticswitch may cause the resulting hierarchy of selenoproteinssynthesized.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Zusätzliche Informationen: BAYCEER105181
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Biologie > Lehrstuhl Ökologische Mikrobiologie
Forschungseinrichtungen > Forschungszentren > Bayreuther Zentrum für Ökologie und Umweltforschung - BayCEER
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Biologie
Forschungseinrichtungen
Forschungseinrichtungen > Forschungszentren
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik
Eingestellt am: 29 Jul 2015 05:53
Letzte Änderung: 11 Feb 2021 08:53
URI: https://eref.uni-bayreuth.de/id/eprint/17353