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Your search keyword '"single nucleotide replacement"' showing total 2 results
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2 results on '"single nucleotide replacement"'

1. Point mutation in the stop codon of

Author

Tomomi, Kawakita, Tetsu, Mukai, Mitsunori, Yoshida, Hiroyuki, Yamada, Masaaki, Nakayama, Yuji, Miyamoto, Masato, Suzuki, Noboru, Nakata, Takemasa, Takii, Akihide, Ryo, Naoya, Ohara, and Manabu, Ato

Subjects
Mycobacterium Infections, Mycobacterium avium subspecies hominissuis, sliding motility, single nucleotide replacement, Mutant Chimeric Proteins, Anti-Bacterial Agents, Mycobacterium, Bacterial Proteins, Drug Resistance, Bacterial, Codon, Terminator, Host-Microbe Interaction, Humans, Point Mutation, growth rate, Copper, Genome, Bacterial, Locomotion, Research Article
Abstract

Mycobacterium avium subspecies hominissuis (MAH) is a pathogen that causes various non-tuberculous mycobacterial diseases in humans and animals worldwide. Among the genus, MAH is characterized by relatively slow growth. Here, we isolated a rapidly growing variant of the MAH 104 strain. The variant strain (named N104) exhibited an enhanced growth rate and higher motility compared to the parent MAH 104 strain (P104). Whole-genome sequencing analysis of N104 revealed the loss of the stop codon of MAV_RS14660 due to a single nucleotide replacement, resulting in the substitution of the codon for tryptophan. Notably, exclusion of the stop codon ligated the open reading frames and caused the fusion of two adjacent proteins. A revertant parent strain, in which a mutation was introduced to restore the stop codon, revealed that elimination of the stop codon in MAV_RS14660 was responsible for the N104 phenotype. Furthermore, we analysed the phenotypes of the parent and mutated strains by determining the functions of the MAV_RS14660 and MAV_RS14655 coding regions flanking the stop codon. The mutant strains, expected to express a fusion protein, exhibited increased resistance to antimicrobial drugs and exogenous copper toxicity compared to that of the parent strains. These findings suggest that the fusion of the MAV_RS14660- and MAV_RS14655-encoding regions in the mutant N104 strain could be related to the modified functions of these intrinsic proteins.

Published
2020

2. Point mutation in the stop codon of MAV_RS14660 increases the growth rate of Mycobacterium avium subspecies hominissuis .

Author

Kawakita T, Mukai T, Yoshida M, Yamada H, Nakayama M, Miyamoto Y, Suzuki M, Nakata N, Takii T, Ryo A, Ohara N, and Ato M

Subjects
Anti-Bacterial Agents pharmacology, Bacterial Proteins metabolism, Codon, Terminator genetics, Copper pharmacology, Drug Resistance, Bacterial genetics, Genome, Bacterial genetics, Humans, Locomotion genetics, Mutant Chimeric Proteins genetics, Mutant Chimeric Proteins metabolism, Mycobacterium drug effects, Mycobacterium genetics, Mycobacterium Infections microbiology, Point Mutation, Bacterial Proteins genetics, Mycobacterium growth & development
Abstract

Mycobacterium avium subspecies hominissuis (MAH) is a pathogen that causes various non-tuberculous mycobacterial diseases in humans and animals worldwide. Among the genus, MAH is characterized by relatively slow growth. Here, we isolated a rapidly growing variant of the MAH 104 strain. The variant strain (named N104) exhibited an enhanced growth rate and higher motility compared to the parent MAH 104 strain (P104). Whole-genome sequencing analysis of N104 revealed the loss of the stop codon of MAV_RS14660 due to a single nucleotide replacement, resulting in the substitution of the codon for tryptophan. Notably, exclusion of the stop codon ligated the open reading frames and caused the fusion of two adjacent proteins. A revertant parent strain, in which a mutation was introduced to restore the stop codon, revealed that elimination of the stop codon in MAV_RS14660 was responsible for the N104 phenotype. Furthermore, we analysed the phenotypes of the parent and mutated strains by determining the functions of the MAV_RS14660 and MAV_RS14655 coding regions flanking the stop codon. The mutant strains, expected to express a fusion protein, exhibited increased resistance to antimicrobial drugs and exogenous copper toxicity compared to that of the parent strains. These findings suggest that the fusion of the MAV_RS14660 - and MAV_RS14655 -encoding regions in the mutant N104 strain could be related to the modified functions of these intrinsic proteins.

Published
2021
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