Characterization of a Unique MutantlysEGene, Originating fromCorynebacterium glutamicum, Encoding a Product That InducesL -Lysine Production inMethylophilus methylotrophus
Author(s) -
Yoshiya Gunji,
Hisao Ito,
Haruhiko Masaki,
Hisashi Yasueda
Publication year - 2006
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60339
Subject(s) - corynebacterium glutamicum , open reading frame , methylotroph , mutant , biology , lysine , gene , biochemistry , start codon , gene product , genetics , amino acid , gene expression , peptide sequence , messenger rna
lysE24 is an allele of lysE encoding an L-lysine exporter of Corynebacterium glutamicum. The mutant gene is able to induce L-lysine production in Methylophilus methylotrophus. Although lysE24 has a mutation in the middle of lysE that results in chain termination, the entire lysE locus, including the region downstream of the short open reading frame, is necessary for L-lysine production. We propose that separate polypeptides are synthesized from the lysE24 locus due to reinitiation of translation utilizing an existing start codon beyond the site of the frameshift, and present evidence that translational coupling is required to form the functional lysE24 product. In addition, expression of lysE24 induces L-lysine production in another methylotroph, Methylobacillus glycogenes. These data suggest that the lysE24 product is a split protein and that this curious feature might be a structure necessary for its functioning in certain obligate gram-negative methylotrophs.
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