FP5 Factor, an Undescribed Sex Factor of <i>Pseudomonas aeruginosa</i>

Matsui, Hideki; Tazaki, Tadakatu

doi:10.1111/j.1348-0421.1973.tb00792.x

Cited by 27 publications

(14 citation statements)

References 16 publications

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“…Mapping of bra-310 locus. Conjugation experiments mediated by plasmid R68.45 (9) or FP5 (20) were carried out to determine the approximate location of bra-310 on the chromosome of P. aeruginosa PAO. Resistance to azaleucine (10 ,ug/ml) was employed as a phenotypic marker of the bra-310 mutation, so that auxotrophic markers such as leu, ilv, or thr were not available for unselected markers.…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a Pseudomonas aeruginosa PAO mutant defective in the structural gene for the LIVAT-binding protein

Hoshino¹,

Nishio²

1982

J Bacteriol

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A mutant of Pseudomonas aeruginosa PAO which has a defect in the structural gene for a binding protein for leucine, isoleucine, valine, alanine, and threonine (LIVAT-binding protein) was isolated and characterized. DL-4-azaleucine was taken up via the high-affinity branched-chain amino acid transport system (LIV-I), but not via the low affinity system (LIV-II), and then inhibited the growth of P. aeruginosa cells. This finding enabled us to select mutants defective in the LIV-I transport system alone. Among such mutants, strain PAO3530 was found to produce an altered LIVAT-binding protein. The shock fluid of this strain contained a normal level of the protein which corresponded to the wild-type LIVAT-binding protein as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by an immunological test. However, the shock fluid showed almost no binding activity for branched-chain amino acids, suggesting that strain PAO3530 has a defect in the structural gene for the LIVAT-binding protein. The mutation locus (bra-310) was mapped in a region between cnu-9001 and oru-325 on the chromosome of P. aeruginosa PAO by conjugation mediated by plasmid FP5 or R68.45.

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Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a Pseudomonas aeruginosa PAO mutant defective in the structural gene for the LIVAT-binding protein

Hoshino¹,

Nishio²

1982

J Bacteriol

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“…Such a multiple mode of existence of the mating genes seems not to be specific to mycobacteria. For instance, in Pseudomonas aeruginosa, three different mating factors (FP 2, FP 5 and FP 39) have been reported [3,4,9], and certain R factors have been shown to promote chromosome transfer [1 1].…”

Section: Discussionmentioning

confidence: 99%

Multiple Mating Types of Mycobacterium smegmatis

Mizuguchi

Suga

Tokunaga

1976

Japanese Journal of Microbiology

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Section: Methodsmentioning

confidence: 99%

“…Phages F116L and G101 were used for transduction (21,23), and phages E79tv-1 and aeruginocin AP41 were used for susceptibility tests (25). Plasmid FP5 with chromosome mobilization ability was used for conjugation (24).Media. Antibiotic medium 3, Mueller-Hinton agar, Mueller-Hinton broth, Proteose Peptone, and nutrient agar were purchased from Difco Laboratories, Detroit, Mich. L broth, L agar, and minimal medium (citrate-free minimal A medium) were as described previously (13,30).…”

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Mutations producing resistance to norfloxacin in Pseudomonas aeruginosa

Hirai¹,

Suzue²,

Irikura³

et al. 1987

Antimicrob Agents Chemother

186

164

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Two genetically distinct classes of norfloxacin-resistant Pseudomonas aeruginosa PA04009 mutants were isolated spontaneously. Two norfloxacin resistance genes, nfxA and nfxB, were mapped between hex-9001 and leu-9005 and between pro-9031 and ilv-9023, respectively, on the P. aeruginosa PAO chromosome. The nfxA gene was shown to be an allele of nalA by transductional analysis with bacteriophage F116L. The nfxB mutant showed a 16-fold increase in resistance to norfloxacin and a slight increase in resistance to nalidixic acid. The nfxB mutant was unique in that it showed hypersusceptibility to beta-lactam and aminoglycoside antibiotics. This mutant had about a threefold-lower rate of norfloxacin uptake than that of the wild-type strain or nfxA mutant. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of outer membrane proteins demonstrated the appearance of a 54,000-dalton protein in the nfxB mutant. These findings suggested that the norfloxacin resistance mechanism in the nfxB mutant might be an alteration in outer membrane permeability to norfloxacin.Norfloxacin and other new 4-quinolones show potent antibacterial activity against gram-negative and grampositive bacteria (11,14,20). They also have high in vitro and in vivo antibacterial activity against Pseudomonas aeruginosa strains that show a strong intrinsic resistance to various antimicrobial agents including older quinolones such as nalidixic acid (11,20,42). The high antibacterial activity of new quinolones might be due to their strong inhibitory action against DNA gyrase, a target enzyme of quinolones, which has been isolated from various bacteria including Pseudomonas aeruginosa (5,16,26,28,42).Drug resistance mediated by plasmids or transposons is a serious clinical problem. However, resistance to nalidixic acid and other quinolones in bacteria is due to chromosomal mutations (10,13,(16)(17)(18)32). Plasmids or transposons that carry quinolone resistance genes have not been found in bacteria (4). Several chromosomal mutations, gyrA, nalB, nalC (gyrB), and nalD, conferring nalidixic acid resistance were identified and mapped on the Escherichia coli K-12 chromosome (10,17,18). Recently, we (13) and Hooper et al. (16) identified norfloxacin resistance mutations (norA, norB, norC, nfxA, and nfxB) in E. coli K-12. norA and nfxA were alleles of gyrA encoding the A subunit of DNA gyrase, while norB, norC, and nfxB determined outer membrane permeability resistance to norfloxacin, were associated with a decrease in OmpF porin protein, and were mapped at 34 min, near 8 min, and at 20 to 22 min, respectively (13, 16). Two loci coding for resistance to nalidixic acid, nalA and nalB, have also been mapped on the P. aeruginosa PAO chromosome (32). It has been reported that DNA replication is resistant to nalidixic acid in permeabilized cells of nalA mutants and that nalB mutants cause a decrease of cell permeability to nalidixic acid and carbenicillin (32).To gain information on the resistance mechanisms to norfloxacin in P. aeruginosa, we isolated spontaneous...

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FP5 Factor, an Undescribed Sex Factor of Pseudomonas aeruginosa

Cited by 27 publications

References 16 publications

Isolation and characterization of a Pseudomonas aeruginosa PAO mutant defective in the structural gene for the LIVAT-binding protein

Isolation and characterization of a Pseudomonas aeruginosa PAO mutant defective in the structural gene for the LIVAT-binding protein

Multiple Mating Types of Mycobacterium smegmatis

Mutations producing resistance to norfloxacin in Pseudomonas aeruginosa

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