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

Title data

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. Vol. 82 (2011) Issue 3 . - pp. 734-747.
ISSN 1365-2958
DOI: https://doi.org/10.1111/j.1365-2958.2011.07850.x

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: BAYCEER105181
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Ecological Microbiology
Research Institutions > Research Centres > Bayreuth Center of Ecology and Environmental Research- BayCEER
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Research Institutions
Research Institutions > Research Centres
Result of work at the UBT: Yes
DDC Subjects: 500 Science
Date Deposited: 29 Jul 2015 05:53
Last Modified: 10 Mar 2016 09:29
URI: https://eref.uni-bayreuth.de/id/eprint/17353