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1.
Genetics and physiology of colicin-tolerant mutants of Escherichia coli 总被引:87,自引:52,他引:35
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A series of colicin-tolerant (tol) mutants of Escherichia coli K-12, which adsorbed colicins but were not killed by them, were isolated and studied genetically and physiologically. Three major classes of mutants were found: tol II, tolerant to colicins A, E1, E2, E3, and K; tol III, tolerant to A, E2, E3, and K; and tol VIII, tolerant to E1 only. The sites of tol II and tol III mutations mapped near the gal region (gene order: tol-gal-bio) and were cotransduced with gal by P1. In heterozygous diploids, tol(+) was dominant over tol; tol II and tol III gave full complementation. All the tol mutations that mapped near gal rendered the bacteria more fragile during growth and hypersensitive to deoxycholate and to ethylenediaminetetraacetic acid. The tol VIII mutation mapped between str and his. These mutants were extremely sensitive to deoxycholate and were also hypersensitive to methylene blue, acridines, and various other compounds. The sensitivity is attributed to increased uptake due to selective alteration of the permeability barrier. The colicin-tolerant mutations are interpreted as affecting some components of the cytoplasmic membrane which mediate between the adsorbed colicin molecules and the target sites of their biochemical effects in the bacterial cell. 相似文献
2.
The insensitivity ofCitrobacter freundii to the E colicins is based on tolerance to colicin E1 and resistance to colicins E2 and E3. Spontaneous colicin A resistant
mutants ofC. freundii also lost their colicin E1 receptor function. Sensitivity to colicin E1 can be induced by F′gal
+
tol
+ plasmids, thetol A+ gene product of which is responsible for this effect.
Receptor function for colicins E2 and E3 is induced by theE. coli F′14bfe
+ plasmid, which is also able to enhance notably the receptor capacity for colicin E1. Thebfe
+ gene product ofE. coli, which is responsible for these phenomena, also restores the receptor function for colicin A and E1 in colicin A resistant
mutants ofC. freundii. All results show that there is a remarkable difference between theE. coli bfe
+ gene product and thebfe
+ gene product ofC. freundii and also between thetol A+ gene products of these strains. The sensitivity to phage BF23 parallels the sensitivity to colicins E2 and E3 and is also
induced by the F′14bfe
+ plasmid. 相似文献
3.
Thirty eight mutant clones of the colicin indicator strainEscherichia coli K 12 ROW, selected by their insensitivity to any of the colicins El–E7, were isolated. Comparison of their sensitivity-resistance patterns to colicins El–E7 enabled us to draw a rough preliminary map of the receptor for E colicins. In this receptor, the highly specific binding site for colicin El partially overlaps with the domain shared by all colicins E2 through E7. A specific binding site of this domain appears to be common for colicins E3 and E6; a part of the E3 and E6 binding site is also common for colicins E4 and E5 and a small, least specific, part also for colicins E2 and E7. Using colicin assay experiments, the binding capacity of coliein E receptor mutants could be estimated. A decreased, but not completely lost ability of certain mutants to bind colicins E, correlated to their lowered sensitivity to them, was found. Thus the phenomenon of partial colicin resistance was established, showing that colicin sensitivity—resistance is not a qualitative but a quantitative marker. 相似文献
4.
Genes affecting coliphage BF23 and E colicin sensitivity in Salmonella typhimurium. 总被引:4,自引:3,他引:1
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Rough strains of Salmonella typhimurium were sensitive to coliphage BF23. Spontaneous mutants resistant to BF23 (bfe) were isolated, and the trait was mapped using phage P1. The bfe gene in S. typhimurium was located between argF (66% co-transducible) and rif (61% co-transducible). The BF23-sensitive S. typhimurium strains were not sensitive to the E colicins. Cells of these rough strains absorbed colicin, as measured by loss of E2 or E3 killing units from colicin solutions and by specific adsorption of 125I-colicin E2 to bfe+ cells. Sensitivity to colicins E1, E2, and E3 was observed in a S. typhimurium strain carrying the F'8 gal+ episome. This episome complemented the tolB mutation of Escherichia coli. We conclude that the bfe+ protein satisfies requirements for adsorption of both phage BF23 and the E colicins. In addition, expression of a gene from E. coli, possibly tolB, is necessary for efficient E colicin killing of S. typhimurium. 相似文献
5.
Colicin A-insensitive mutants ofCitrobacter freundii were isolated and grouped into six phenotypic classes characterized by sensitivity, insensitivity or partial insensitivity to the bacteriocins S6, DF 13 and colicin A, and sensitivity or insensitivity to deoxycholate (DOC) and ampicillin. Mapping by the gradient-of-transmission method revealed the chromosomal regions in which the responsible genes are situated. Res-3 mapped nearpur betweenpur andthr; Tol-5 mapped betweenaro andilv and Tol-4 betweengal andpyr; Tol-1, Tol-2 and Tol-3 are situated close togal. All the mutations that mapped neargal rendered the bacteria more sensitive to DOC and ampicillin. Complementation analysis withE. coli plasmids showed that the three phenotypic groups that map neargal were complemented byE. coli plasmids and fall into three complementation groups. Two of these are equivalent with thetol A andtol B genes inE. coli. 相似文献
6.
Sensitivity of spheroplasts (prepared in two ways) of a colicin-sensitive strain, of colicinresistant and of colicin-tolerant
mutants and of strains immune to colicins E1 and E2 was estimated and compared. Generally, the removal of the peptidoglycan
layer brought about a slight nonspecific support for colicin translocation across the cell wall in sensitive,tolB tolerant and immune bacteria.tolB spheroplasts were colicin E1-sensitive, but E2-insensitive. Spheroplasts were always fragile and lysed spontaneously, especially
those produced by lysozyme. Bacteria carryingtolA, tolQ andtolR mutations kept their colicin insensitivity as spheroplasts, just as the resistant ones. Bacteria rendered colicinogenic and
hence colicin-immune turned to high colicin sensitivity in spheroplast form. The results indicate a change in plasma membrane
associated with the spheroplast formation. 相似文献
7.
Colicin E-resistant mutants were isolated in Escherichia coli K-12 which, although still apparently possessing the E receptor and adsorbing colicin, were nevertheless insensitive (refractory) to its effect. Eight phenotypic groups were obtained, but some mutants from three of these groups were all shown to map at gal, whereas a second refractory locus, giving resistance to E1 alone, mapped close to thy. It is suggested that the successful fixation of any of the three distinct colicins of group E may involve a dual role for the cell surface "receptor," the first for the binding of the protein and the second for the correct orientation of the bound molecule relative to the cytoplasmic membrane. The majority of the refractory mutants isolated may derive from changes in components concerned with the second of these receptor functions. Two groups of mutants, however, refractory to only E1 or E2, probably reflect changes in the intracellular transmission systems which specifically mediate the effects of these two colicins, the changes not allowing transmission through the cytoplasmic membrane to the respective targets of the colicins. The E1 adsorption site was shown to be distinct from that for E2 and E3, indicating an early separation of the colicin E transmission systems. 相似文献
8.
S. James L. Cariss Chrystala Constantinidou Mala D. Patel Yuiko Takebayashi Jon L. Hobman Charles W. Penn Matthew B. Avison 《Journal of bacteriology》2010,192(13):3329-3336
Colicin E2-tolerant (known as Cet2) Escherichia coli K-12 mutants overproduce an inner membrane protein, CreD, which is believed to cause the Cet2 phenotype. Here, we show that overproduction of CreD in a Cet2 strain results from hyperactivation of the CreBC two-component regulator, but CreD overproduction is not responsible for the Cet2 phenotype. Through microarray analysis and gene knockout and overexpression studies, we show that overexpression of another CreBC-regulated gene, yieJ (also known as cbrC), causes the Cet2 phenotype.Colicins are protein antibiotics that have various modes of action. They are usually encoded on plasmids and, in many cases, alongside genes encoding colicin immunity factors, which protect colicin-producing cells from the colicin they produce. Of the enzymatic (E) colicins, some carry nuclease activity, including colicin E2, colicin E9, and colicin E3. These three proteins bind to susceptible cells via the surface protein BtuB (the vitamin B12 importer) and, through a series of events that are poorly understood, cross the cell envelope to enter the cytoplasm, where they degrade nucleic acids: colicins E2 and E9 target DNA; colicin E3 targets rRNA (11).Cells can readily become tolerant of E colicins. Mutants usually have lost either the colicin receptor or some protein involved in colicin import. Loss-of-function mutations in btuB confer tolerance of high levels of colicins E2, E9, and E3. Almost 40 years ago, Escherichia coli mutants having a colicin E2-tolerant (Cet2) phenotype were identified. The Cet2 phenotype confers tolerance of colicins E2 and E9 only, while cells remain susceptible to colicin E3, and BtuB is intact (8, 9). Cet2 mutants were shown to overproduce an inner membrane protein (26), and the cet2 mutation was found to be dominant in trans and mapped at 99.9 min on the E. coli chromosome (8, 9). Using the Cet2 mutant RB208 as a source of genomic DNA, a clone able to transform E. coli cells to a Cet2 phenotype was identified. Since this clone carried a gene predicted to encode an inner membrane protein with properties identical to those overproduced in Cet2 mutants, the gene was named cet (15).The cet gene is the last gene in the four-gene cre locus, so cet is also known as creD. The other genes in this locus are creA (hypothetical open reading frame [ORF]); creB, encoding a response regulator; and creC, encoding a sensor kinase. CreB and CreC form a classical two-component regulatory system, and we recently showed that CreBC are activated upon fermentation of glucose in minimal medium or during aerobic growth on minimal medium containing fermentation products, such as pyruvate, lactate, or acetate, as the sole carbon and energy source (10). CreBC controls the expression of a number of genes (the Cre regulon), some of which encode metabolic functions but several of which are hypothetical. One of the most tightly controlled Cre regulon genes is creD (5).We have previously shown that the Cet2 strain RB208 has a point mutation in creC but that creD itself is wild type (5). Since the RB208 genomic clone capable of transforming cells to a Cet2 phenotype carries the whole cre locus, not just creD (15), our hypothesis is that the Cet2 phenotype of the transformant was due to a trans-dominant mutation in the cloned creC mutant allele activating one or more Cre regulon genes and that the Cet2 phenotype may or may not be caused by overexpression of creD. The aims of the experiments described in this paper were to test our hypothesis that the Cet2 phenotype is caused by activating mutations in CreBC and to definitively identify the Cre regulon gene that encodes the colicin E2 tolerance (Cet) protein. 相似文献
9.
Isolation and characterization of an Escherichia coli mutant tolerant to colicins Ia and Ib 总被引:16,自引:8,他引:8
Two classes of spontaneous colicin I insensitive mutants of Escherichia coli have been isolated. The first class (called cir) has lost its ability to adsorb either colicin Ia or Ib, maps at 41 min on the E. coli genetic map, and retains sensitivity to all other colicins tested. The cir phenotype is probably due to an alteration in the colicin I receptor. The second class of mutant (called tolI) retains full capacity to adsorb [(125)I]colicin I and, therefore, represents the isolation of a mutant tolerant to colicin I. The tolI mutant is sensitive to all other colicins tested and has a map location of 89-1 min. The tolI mutant grows with a reduced mass yield when glucose is used as a carbon source and cannot utilize succinate or acetate for growth. The tolI mutant shows a reduced sensitivity to sodium azide and phenethylalcohol. It is suggested that tolI is deficient in some aspect of aerobic metabolism which must be operative for colicin I sensitivity. 相似文献
10.
Michael Feldgarden Margaret A. Riley 《Evolution; international journal of organic evolution》1999,53(4):1019-1027
Previous studies indicate that most natural isolates of Escherichia coli are resistant to most or all colicins (antibiotics produced by E. coli) when assessed in the laboratory. Additionally, resistance to different colicin types appears to arise in a nonindependent manner. One possible mechanism to explain this nonindependence is pleiotropy: Multiple resistances are selected after exposure to a single colicin. This study, which was designed to address the role of pleiotropy in the generation of colicin resistance, revealed that 96% of colicin resistant mutants were resistant to two or more colicins. Mutational class was important because putative translocation mutants (Tol pathway mutants) resisted fewer colicins than putative receptor mutants. To determine whether colicin resistance is costly, the effects of colicin resistance mutations on maximal growth rate in a rich medium were also examined. Relative to the sensitive ancestor, translocation mutations lowered maximal growth rates by 17%, whereas putative receptor mutations did not significantly lower growth rates. Thus, when nutrients are abundant, the most advantageous forms of colicin resistance may not impose a cost. The ecological consequences of pleiotropic colicin resistance could involve population cycling between colicin sensitivity and resistance. Additionally, if the cost of resistance depends on the environment, ecological diversification could result. 相似文献
11.
The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step 总被引:5,自引:2,他引:3
Emmanuelle Bouveret Alain Rigal Claude Lazdunski & Hélène Bénédetti 《Molecular microbiology》1997,23(5):909-920
Colicins use two envelope multiprotein systems to reach their cellular target in susceptible cells of Escherichia coli : the Tol system for group A colicins and the TonB system for group B colicins. The N-terminal domain of colicins is involved in the translocation step. To determine whether it interacts in vivo with proteins of the translocation system, constructs were designed to produce and export to the cell periplasm the N-terminal domains of colicin E3 (group A) and colicin B (group B). Producing cells became specifically tolerant to entire extracellular colicins of the same group. The periplasmic N-terminal domains therefore compete with entire colicins for proteins of the translocation system and thus interact in situ with these proteins on the inner side of the outer membrane. In vivo cross-linking and co-immunoprecipitation experiments in cells producing the colicin E3 N-terminal domain demonstrated the existence of a 120 kDa complex containing the colicin domain and TolB. After in vitro cross-linking experiments with these two purified proteins, a 120 kDa complex was also obtained. This suggests that the complex obtained in vivo contains exclusively TolB and the colicin E3 domain. The N-terminal domain of a translocation-defective colicin E3 mutant was found to no longer interact with TolB. Hence, this interaction must play an important role in colicin E3 translocation. 相似文献
12.
Genetics of Sensitivity of Salmonella Species to Colicin M and Bacteriophages T5, T1, and ES18
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Nearly all of 62 strains of Salmonella paratyphi B were sensitive to colicin M and phage T5 but resistant to phages T1 and ES18 and to colicin B. All tested S. typhimurium strains were resistant to colicin M and phage T5, and many were sensitive to phage ES18. A rough S. typhimurium LT2 strain given the tonA region of Escherichia coli or S. paratyphi B became sensitive to colicin M and phage T5. We infer that the tonA allele of S. paratyphi B, like that of E. coli, determines an outer membrane protein that adsorbs T5 and colicin M but not phage ES18, whereas the S. typhimurium allele determines a protein able to adsorb only ES18. The partial T1 sensitivity of a rough LT2 strain with a tonA allele from E. coli or S. paratyphi B and also the tonB(+) phentotype of an E. coli B trp-tonB Delta mutant carrying an F' trp of LT2 origin showed that S. typhimurium LT2 has a tonB allele like that of E. coli with respect to determination of sensitivity to colicins and phage T1. Rough S. paratyphi B, although T5 sensitive, remained resistant to T1 even when given F' tonB(+) of E. coli origin. Classes of Salmonella mutants selected as resistant to colicin M included: T5-resistant mutants, probably tonA(-); mutants unchanged except for M resistance, perhaps tolerant; and Exb(+) mutants, producing a colicin inhibitor (presumably enterochelin). Some Exb(+) mutants were resistant to a bacteriocin inactive on E. coli but active on all tested S. paratyphi B and S. typhimurium strains (and on nearly all other tested Salmonella). A survey showed sensitivity to colicin M in several other species of Salmonella. 相似文献
13.
Escherichia coli strains B and K12 W 1655 F+ are able to bind more lethal units of colicins E2, E3, G, H, Ia, and K+ X per one stable L-form cell (of the protoplast type) than per one rod cell; colicin D is bound in a higher amount on E. coli B rods. This pattern remains unchanged, if the same colicins are attached on chloroform-killed cells of both forms. Rods of both E. coli strains are more sensitive to colicins D, E2, E3, K + X (as--in the strain B--to colicin Ia) than cells of the respective L-forms. In the strain W 1655 F+ both cell forms are equally highly sensitive to colicin Ia. The stable L-forms of both strains are much more sensitive to colicins G and H than the rods. Thus the Gram-negative cell wall decreases the probability of a colicin molecule to get attached to its receptor in the cytoplasmic membrane. On the other hand, in E. coli cells the attachment of most colicin molecules to the wall receptors increases the probability of their biological effect. There is no such effect of the wall-attachment on the action of colicins G or H. The strain B is tolerant to colicin E2, while being resistant to E3; thus the cytoplasmic membrane receptor sites for them are not identical. 相似文献
14.
The TolA protein interacts with colicin E1 differently than with other group A colicins. 总被引:3,自引:0,他引:3
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The 421-residue protein TolA is required for the translocation of group A colicins (colicins E1, E2, E3, A, K, and N) across the cell envelope of Escherichia coli. Mutations in TolA can render cells tolerant to these colicins and cause hypersensitivity to detergents and certain antibiotics, as well as a tendency to leak periplasmic proteins. TolA contains a long alpha-helical domain which connects a membrane anchor to the C-terminal domain, which is required for colicin sensitivity. The functional role of the alpha-helical domain was tested by deletion of residues 56 to 169 (TolA delta1), 166 to 287 (TolA delta2), or 54 to 287 (TolA delta3) of the alpha-helical domain of TolA, which removed the N-terminal half, the C-terminal half, or nearly the entire alpha-helical domain of TolA, respectively. TolA and TolA deletion mutants were expressed from a plasmid in an E. coli strain producing no chromosomally encoded TolA. Cellular sensitivity to the detergent deoxycholate was increased for each deletion mutant, implying that more than half of the TolA alpha-helical domain is necessary for cell envelope stability. Removal of either the N- or C-terminal half of the alpha-helical domain resulted in a slight (ca. 5-fold) decrease in cytotoxicity of the TolA-dependent colicins A, E1, E3, and N compared to cells producing wild-type TolA when these mutants were expressed alone or with TolQ, -R, and -B. In cells containing TolA delta3, the cytotoxicity of colicins A and E3 was decreased by a factor of >3,000, and K+ efflux induced by colicins A and N was not detectable. In contrast, for colicin E1 action on TolA delta3 cells, there was little decrease in the cytotoxic activity (<5-fold) or the rate of K+ efflux, which was similar to that from wild-type cells. It was concluded that the mechanism(s) by which cellular uptake of colicin E1 is mediated by the TolA protein differs from that for colicins A, E3, and N. Possible explanations for the distinct interaction and unique translocation mechanism of colicin E1 are discussed. 相似文献
15.
Escherichia coli K-12 tolZ mutants tolerant to colicins E2, E3, D, Ia, and Ib: defect in generation of the electrochemical proton gradient 总被引:2,自引:0,他引:2
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Spontaneous Escherichia coli K-12 mutants tolerant to colicin E3 were isolated, and on the basis of their tolerance patterns to 19 kinds of colicins, a new phenotypic class of tolZ mutants was found. The tolZ gene was located between min 77 and 78 on the E. coli K-12 genetic map. The tolZ mutants were tolerant to colicins E2, E3, D, Ia, and Ib, and showed an increased sensitivity to ampicillin, neomycin, and EDTA, but not to deoxycholate; they were able to grow on glucose minimal medium, but not on nonfermentable carbon sources (succinate, acetate, pyruvate, lactate, malate, etc.). The pleiotropic phenotype of the tolZ mutant was due to a single mutation. Both respiration and membrane ATPase activity of the tolZ mutant were normal. The tolZ mutant had a defect in the uptake of proline, glutamine, thiomethyl-beta-D-galactoside, and triphenylmethylphosphonium ion; these uptake systems are driven by an electrochemical proton gradient (delta-mu H+) or a membrane potential (delta psi). In contrast, the uptake of methionine and alpha-methyl-D-glucoside, which is not dependent on delta-mu H+ and delta psi, was normal in the tolZ mutant. Glucose 6-phosphate uptake at pH 5.5, which is driven by a transmembrane pH gradient, in the tolZ mutant was similar to the parent level. These results indicate that the tolZ mutant has a defect in the generation of delta-mu H+ and delta psi. 相似文献
16.
Emmanuelle Bouveret Alain Rigal Claude Lazdunski & Hélène Bénédetti 《Molecular microbiology》1998,27(1):143-157
Group A colicins need proteins of the Escherichia coli envelope Tol complex (TolA, TolB, TolQ and TolR) to reach their cellular target. The N-terminal domain of colicins is involved in the import process. The N-terminal domains of colicins A and E1 have been shown to interact with TolA, and the N-terminal domain of colicin E3 has been shown to interact with TolB. We found that a pentapeptide conserved in the N-terminal domain of all group A colicins, the 'TolA box', was important for colicin A import but was not involved in the colicin A–TolA interaction. It was, however, involved in the colicin A–TolB interaction. The interactions of colicin A N-terminal domain deletion mutants with TolA and TolB were investigated. Random mutagenesis was performed on a construct allowing the colicin A N-terminal domain to be exported in the bacteria periplasm. This enabled us to select mutant protein domains unable to compete with the wild-type domain of the entire colicin A for import into the cells. Our results demonstrate that different regions of the colicin A N-terminal domain interact with TolA and TolB. The colicin A N-terminal domain was also shown to form a trimeric complex with TolA and TolB. 相似文献
17.
Jordan Konisky Billie S. Cowell Mary J. Gilchrist 《Journal of cellular biochemistry》1973,1(3):208-219
The specific binding of 125 Iodine labelled colicin Ia and Ib to Escherichia coli cell envelopes and partially purified cell walls is demonstrated. Neither partially purified cytoplasmic membranes isolated from a wild type sensitive strain nor envelopes or cell walls prepared from an E. coli mutant known to be defective in the colicin I receptor could bind the colicins. Competition studies suggest that colicins Ia and Ib have a common bacterial receptor which resides in the bacterial cell wall. 相似文献
18.
J. Šmarda 《Folia microbiologica》1975,20(3):264-271
According to the theory of Fredericq (1949) and Nomura (1964), colicins are attached by specific receptor sites in the cell walls of sensitive bacteria, which mediate their inhibitive effects. During last years, a great variety of experimental data have been accumulated, some of which cannot be easily interpreted in terms of this theory. There exist considerable discrepancies concerning the chemical nature and molecular weight of isolated receptors. The attachment of a colicin onto its receptor need not be irreversible. The inhibition of numerous membrane-associated functions in colicin-tolerant mutants suggests their pleiotropic deletion nature. The difference between colicin resistance and colicin tolerance does not seem to be clear-cut. Cells of stable L-forms of protoplast type, completely devoid of their walls, retain in most cases the same patterns of sensitivity to colioins as rods of the same strains. Experimental changes in the relationship between the cell wall and the cytoplasmic membrane decrease colicin sensitivity of the cells. Colicin E3 has been found to be a specific endoribonuclease, able to cleave a terminal fragment from the 16 S rRNA also in isolated ribosomesin vitro: not only in ribosomes from sensitivive bacteria, but also in those from resistant ones and from eukaryotic cells. A destabilization of the DNA helix was induced by colicin E2in vitro asin vivo. It seems that there exist two distinct types of colicin receptors with different functions: those in the cell wall, and those in the cytoplasmic membrane. Only the contact of colicins with the latter ones is biologically effective and starts both stages of their inhibitive effect: the reversible and the irreversible ones. 相似文献
19.
20.
Cross-resistance between bacteriophages and colicins in Escherichia coli K-12. 总被引:5,自引:5,他引:0
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Cross-resistance between bacteriophages and colicins was studied using collections of bacteriophage- and colicin-resistant mutants of Escherichia coli K-12. No new examples were found of highly specific one-to-one cross-resistance of the type suggestive of common receptors. However, several groups of mutants showed tolerance to colicins and resistance to bacteriophages. Mutants known to be very defective in lipopolysaccharides composition were found to commonly show tolerance to certain colicins in addition to their bacteriophage resistance. Another group of mutants showed varying patterns of resistance to colicins E2, E3, K, L, A, S4, N, and X and bacteriophages E4, K2, K20, K21, K29, and H+. However, many bacteriophage-resistant mutants were fully colicin sensitive, and most colicin-resistant mutants were fully sensitive to bacteriophages. 相似文献