Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae

DNA Research : an International Journal for Rapid Publication of Reports on Genes and Genomes
K EnomotoHaruhiro Muratsubaki

Abstract

A gene of the soluble fumarate reductase (FRDS) that binds FAD non-covalently was cloned by polymerase chain reaction (PCR) using degenerate oligonucleotides designed from partial amino acid sequences of highly purified enzyme. The nucleotide sequence of a 0.99-kb amplified product was found to be nearly identical to a partial sequence of an open reading frame (ORF) previously reported (EMBL database accession number S-30830). According to the sequence in the EMBL database, we cloned 1.7-kb fragment containing entire sequence of this ORF by PCR and found that this fragment contained a perfect match to the 0.99-kb sequence amplified with the degenerate primers. From these results, we concluded that this ORF is the FRDS gene. The amino acid sequences of the regions involved in the non-covalent binding of FAD and the active site, which are conserved among the flavoprotein subunits of membrane-bound fumarate reductase and succinate dehydrogenase, were found in FRDS. However, unlike the membrane-bound enzymes, FRDS did not contain the histidine residue that covalently binds the isoalloxazine ring of FAD at or near the corresponding position. FRDS showed high homology to the product of S. cerevisiae OSM1 gene which was reported to be...Continue Reading

Citations

Jul 24, 2003·Mechanisms of Ageing and Development·Suzan J Holt, Donald L Riddle
Oct 24, 2002·FEMS Microbiology Letters·Keiichiro EnomotoHaruhiro Muratsubaki
Feb 22, 2012·Fungal Genetics and Biology : FG & B·Kinga A SędzielewskaGotthard Kunze
Jun 1, 2005·Microbial Cell Factories·Anna WojtowiczAndrzej Plucienniczak
Aug 21, 2012·FEMS Yeast Research·Kinga A SędzielewskaGotthard Kunze
Jan 24, 2013·PloS One·Mayumi HachinoheHiroshi Masumoto
May 10, 2015·DNA Repair·James M DaleyPatrick Sung
Jan 22, 2017·Applied Microbiology and Biotechnology·Jiaojiao LiQingsheng Qi
Dec 11, 2019·Proceedings of the National Academy of Sciences of the United States of America·Samuel H LightDaniel A Portnoy
May 20, 1998·Archives of Biochemistry and Biophysics·H Muratsubaki, K Enomoto
Oct 20, 2005·Journal of Bioscience and Bioengineering·Y ArikawaM Okazaki

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