Coordinated alterations in ribosomes and cytoplasmic membrane in sucrose-dependent, spectinomycin-resistant mutants of Escherichia coli

Mizuno, Takeshi; Yamada, H.; Yamagata, Hideo; Mizushima, Shôji

doi:10.1128/jb.125.2.524-530.1976

Cited by 21 publications

(11 citation statements)

References 24 publications

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“…Analysis of cytoplasmic membrane proteins. As previously reported, a protein 1-19 was missing in all cytoplasmic membrane preparations from 10 Sucd Spcr mutants, including YM101 (9). To examine whether this alteration of a membrane component was also a result of mutation in the A53-spcl region, the following experiment was carried out.…”

Section: Ym101 Was Originally Isolated As a Sucd Spcrmentioning

confidence: 91%

“…Preparation and analysis of cytoplasmic membranes. Preparation of cytoplasmic membranes and polyacrylamide gel electrophoresis of membrane proteins were carried out as described previously (9).…”

Section: Methodsmentioning

confidence: 99%

“…To examine whether this alteration of a membrane component was also a result of mutation in the A53-spcl region, the following experiment was carried out. Colonies of strains YMlO1T6r [F'3(X A53)], YM1OlT6r [F'3(X spc2)], and YM1OlT6r [F'3(X fus2)] formed on the M3 plate were grown in M3su broth at 37°C to the late logarithmic phase of growth and analyzed for cytoplasmic membrane proteins by sodium dodecyl sulfate-gel electrophoresis as described previously (9). Figure 3 shows scans of polyacrylamide gels of cytoplasmic membrane proteins of these strains as well as those of W4626phe (parent strain), YM1O1T6r, and YM101T6r [F'3(X spcl)].…”

Section: Ym101 Was Originally Isolated As a Sucd Spcrmentioning

confidence: 99%

“…Furthermore, these mutants are hypersensitive to various antibiotics, dyes, and detergents and show morphological changes, which suggests some alterations of the cell envelope in the mutants (8). Biochemical analysis of the mutants indicates that one of cytoplasmic membrane proteins, I-19, is misi in all cytoplasmic membrane preparations from 10 Sucd SpCr mutants (9). Alterations of 30S ribosomal protein S5, S4, or S3 seems to make the polypeptide synthetic activity of ribosomes of these mutants reistant to spectinomycin (2).…”

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confidence: 98%

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Deletion mapping and heterogenote analysis of a mutation responsible for osmosis-sensitive growth, spectinomycin resistance, and alteration of cytoplasmic membrane in Escherichia coli

Yamagata¹,

Dombou²,

Sato³

et al. 1980

J Bacteriol

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Lambda transducing phages carrying Escherichia coli deoxyribonucleic acid of various lengths from the aroE-rpsL region were lysogenized into the F'3 plasmid and were used for heterogenote analysis of YM101, a sucrose-dependent, spectinomycin-resistant mutant of E. coli. Three characteristics of the mutant strain, resistance to spectinomycin, sucrose dependence of growth, and lack of I-19 protein in the cytoplasmic membrane, were shown to be the result of a mutation in a region designated delta 53-spcl. This region extends over 3.6-kilobase pairs and is located within a cluster of ribosomal genes. The mutation is recessive to the wild-type allele.

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Section: Ym101 Was Originally Isolated As a Sucd Spcrmentioning

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Section: Ym101 Was Originally Isolated As a Sucd Spcrmentioning

confidence: 99%

mentioning

confidence: 98%

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Deletion mapping and heterogenote analysis of a mutation responsible for osmosis-sensitive growth, spectinomycin resistance, and alteration of cytoplasmic membrane in Escherichia coli

Yamagata¹,

Dombou²,

Sato³

et al. 1980

J Bacteriol

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“…It is known that the temperature-dependent elimination of F factors varies with the strain that harbors these factors (22,27,28). In fact, it has been shown that the thermosensitive sex factor Flac+ T62 is influenced very much by a host mutation concerning a ribosomal protein that appears to be related to spectinomycin resistance (16,27,28). These considerations suggest that the temperature-dependent elimination of a plasmid may be greatly influenced by the physiological state of the host bacteria.…”

mentioning

confidence: 99%

Requirement of Cyclic Adenosine 3′,5′-Monophosphate for the Thermosensitive Effects of Rts1 in a Cyclic Adenosine 3′,5′-Monophosphate-Less Mutant of Escherichia coli

1977

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Previous publications showed that a covalently closed circular (CCC) Rtsl plasmid deoxyribonucleic acid (DNA) that confers kanamycin resistance upon the host bacteria inhibits host growth at 420C but not at 32°C. At 42°C, the CCC Rtsl DNA is not formed, and cells without plasmids emerge. To investigate the possible role of cyclic adenosine 3',5'-monophosphate (cAMP) in the action of Rtsl on host bacteria, Rtsl was placed in an Escherichia coli mutant (CA7902) that lacks adenylate cyclase or in E. coli PP47 (a mutant lacking cAMP receptor protein). Rtsl did not exert the thermosensitive effect on these cells, and CCC Rtsl DNA was formed even at 42°C. Upon addition of cAMP to E. coli CA7902(Rtsl), cell growth and formation of CCC Rtsl DNA were inhibited at 42°C. The addition of cAMP to E. coli PP47(Rtsl) did not cause inhibitory effects on either cell growth or CCC Rtsl DNA formation at 420C. The inhibitory effect of cAMP on E. coli CA7902(Rtsl) is specific to this cyclic nucleotide, and other cyclic nucleotides such as cyclic guanosine 3',5'-monophosphate did not have the effect. For this inhibitory effect, cells have to be preincubated with cAMP; the presence of cAMP at the time of CCC Rtsl DNA formation is not enough for the inhibitory effect. If the cells are preincubated with cAMP, one can remove cAMP during the [3H]thymidine pulse and still observe its inhibitory effect on the formation of CCC Rtsl DNA. The presence of chloramphenicol during this preincubation period abolished the inhibitory effect of cAMP. These observations suggest that cAMP is necessary to induce synthesis of a protein that inhibits CCC Rtsl DNA formation and cell growth at 420C. 80 on July 16, 2020 by guest

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The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate.

1989

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Mecillinam, a beta‐lactam antibiotic which binds specifically to penicillin‐binding protein 2 (PBP2), blocks lateral cell‐wall elongation, induces spherical morphology and ultimately kills bacteria. We describe here a new mecillinam‐resistant mutant of Escherichia coli, the lov mutant. It possesses active PBP2, as evidenced by its rod shape in the absence of mecillinam (but not in its presence), its ability to filament when septation is inhibited, and its penicillin‐binding ability. The lov mutant grows slowly but seems to regulate its macromolecular parameters properly: cell volume, RNA content (ribosome concentration), and DNA content are appropriate for the growth rate, and the growth yield is identical to that of wild type. The lov mutation is located at 41 min on the E.coli genetic map and is recessive. Certain rpsL (StrR) mutations suppress the lov mutant's mecillinam resistance. The allele specificity of the suppression suggests that the lov gene product may interact directly with the ribosomes. The lov gene product thus seems to define a link between PBP2 (the mecillinam target) and the ribosomes; we propose that this link is involved in transmitting information on the growth rate (ribosome concentration) to the peptidoglycan synthesizing apparatus.

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Coordinated alterations in ribosomes and cytoplasmic membrane in sucrose-dependent, spectinomycin-resistant mutants of Escherichia coli

Cited by 21 publications

References 24 publications

Deletion mapping and heterogenote analysis of a mutation responsible for osmosis-sensitive growth, spectinomycin resistance, and alteration of cytoplasmic membrane in Escherichia coli

Deletion mapping and heterogenote analysis of a mutation responsible for osmosis-sensitive growth, spectinomycin resistance, and alteration of cytoplasmic membrane in Escherichia coli

Requirement of Cyclic Adenosine 3′,5′-Monophosphate for the Thermosensitive Effects of Rts1 in a Cyclic Adenosine 3′,5′-Monophosphate-Less Mutant of Escherichia coli

The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate.

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