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Analysis of the rates of transcriptional coupling and translational fusion between hydroxylase and rubredoxin subunits of alkane monooxygenase in bacterial genomes
Author(s) -
Masuda Hisako,
Rikard Matthew,
Tupa Peter R
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.612.7
Subject(s) - operon , rubredoxin , monooxygenase , fusion protein , gene , biology , bacteria , bacterial genome size , biochemistry , chemistry , genome , genetics , enzyme , escherichia coli , cytochrome p450 , recombinant dna
Two functionally related proteins typically can be translationally fused to form a large protein or encoded as separate polypeptides, yet share transcriptional regulation by forming an operonic structure. In operon, multiple proteins are encoded from a single transcript, allowing these proteins to be expressed at the relatively fixed stoichiometric ratio. The goal of this study was to assess the relative rate of formation and disassembly of operons (transcriptional coupling) and gene fusions (translational fusion) of the hydroxylase and rubredoxin subunits of alkane monooxygenase in published bacterial genomes. Alkane monooxygenase is a non‐heme diiron oxygenase that catalyzes the initial, rate limiting step of linear alkane metabolism in aerobic bacteria. It is widely found both in gram negative and gram positive bacteria. The relative abundance of various genetic structure of alkane monooxygenases has not been studied previously. Our study indicates that the transcriptional coupling proceeds translational fusion in all detected cases. The rate of disassembly was faster than the formation in both processes. Moreover, the rate of disassembly of operon and fusion occurred at an equivalent rate. The possible biological basis for the faster rate of disassembly and its implications in horizontal gene transfer will be discussed.