Linkage Map of<i>Escherichia coli</i>K-12, Edition 10: The Traditional Map

Berlyn, Mary K. B.

doi:10.1128/mmbr.62.3.814-984.1998

Cited by 226 publications

(80 citation statements)

References 4,853 publications

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“…T4 initially binds to the terminal glucose residue of LPS during infection, and changes in the structure or outright loss of this receptor render cells resistant to infection. The loci lpcA and lpcB are involved in synthesis of the LPS core, as is the set of loci known as rfa (Berlyn 1998). Mutations in any of these loci can produce resistance to T4 infection.…”

Section: T H E C O M M U N I T Y E C O L O G Y O F T -S E R I E S P Hmentioning

confidence: 99%

Linking genetic change to community evolution: insights from studies of bacteria and bacteriophage

2000

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A major goal of community ecology is to link biological processes at lower scales with community patterns. Microbial communities are especially powerful model systems for making these links. In this article, we review recent studies of laboratory communities of bacteria and bacteriophage (viruses that infect bacteria). We focus on the ecology and evolution of bacteriophage-resistance as a case study demonstrating the relationship between specific genes, individual interactions, population dynamics, community structure, and evolutionary change. In laboratory communities of bacteria and bacteriophage, bacteria rapidly evolve resistance to bacteriophage infection. Different resistance mutations produce distinct resistance phenotypes, differing, for example, in whether resistance is partial or complete, in the magnitude of the physiological cost associated with resistance, and in whether the mutation can be countered by a host-range mutation in the bacteriophage. These differences determine whether a mutant can invade, the effect its invasion has on the population dynamics of sensitive bacteria and phage, and the resulting structure of the community. All of these effects, in turn, govern the community's response to environmental change and its subsequent evolution.

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Section: T H E C O M M U N I T Y E C O L O G Y O F T -S E R I E S P Hmentioning

confidence: 99%

Linking genetic change to community evolution: insights from studies of bacteria and bacteriophage

2000

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“…The DNA from each time sample was prepared by centrifugation of the cells at 4500 r.p.m. at 4∞C in a Sorvall RC-3B centrifuge with rotor H600A for 30 min and washed with 5 ml of ice-cold TES (50 mM Tris-HCl, 50 mM NaCl, 5 mM EDTA, © 2002 Blackwell Science Ltd, Molecular Microbiology, 44, 1429-1440 Berlyn (1998). b.…”

Section: Dna Preparationmentioning

confidence: 99%

Eclipse period without sequestration in Escherichia coli

Olsson¹,

Dasgupta²,

Berg³

et al. 2002

Molecular Microbiology

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Summary The classical Meselson–Stahl density shift experiment was used to determine the length of the eclipse period in Escherichia coli, the minimum time period during which no new initiation is allowed from a newly replicated origin of chromosome replication, oriC. Populations of bacteria growing exponentially in heavy (15NH4+ and 13C6‐glucose) medium were shifted to light (14NH4+ and 12C6‐glucose) medium. The HH‐, HL‐ and LL‐DNA were separated by CsCl density gradient centrifugation, and their relative amounts were determined using radioactive gene‐specific probes. The eclipse period, estimated from the kinetics of conversion of HH‐DNA to HL‐ and LL‐DNA, turned out to be 0.60 generation times for the wild‐type strain. This was invariable for widely varying doubling times (35, 68 and 112 min) and was independent of the chromosome locus at which the eclipse period was measured. For strains with seqA, dam and damseqA mutants, the length of the eclipse period was 0.16, 0.40 and 0.32 generation times respectively. Thus, initiations from oriC were repressed for a considerable proportion of the generation time even when the sequestration function seemed to be severely compromised. The causal relationship between the length of the eclipse period and the synchrony of initiations from oriC is discussed.

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“…The latter encodes a multidrug resistance e¥ux protein and the former an inner-membrane lipoprotein associated with the e¥ux protein [6]. In the recent E. coli linkage map [7] they are renamed acrE and acrF, respectively. The acrEF operon was mapped at min 73.5 [8], far from the position where the envC mutation had been mapped, and thus most likely is a multicopy suppressor distinct from the true envC.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity

原

2002

FEMS Microbiology Letters

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PM61 is a chain-forming envC strain of Escherichia coli with a leaky outer membrane. It was found to have an oversized penicillinbinding protein 3, which was the result of an IS4 insertion in the prc gene. The other properties of PM61 were caused by the envC mutation. We cloned the envC (yibP) gene and identified the mutation site, causing a single residue substitution, H366Y, in the PM61 envC allele. The gene product was predicted to be a periplasmic protein having coiled-coil structure in the N-terminal region and homology to lysostaphin in the C-terminal region. Overexpression of envC inhibited cell growth, and overexpression of the PM61 mutant allele caused cell lysis. Disruption of the chromosomal envC caused the same defects as the envC point mutation, indicating the gene is dispensable for growth but important for normal septation/separation and cell envelope integrity. ß

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Linkage Map ofEscherichia coliK-12, Edition 10: The Traditional Map

Cited by 226 publications

References 4,853 publications

Linking genetic change to community evolution: insights from studies of bacteria and bacteriophage

Linking genetic change to community evolution: insights from studies of bacteria and bacteriophage

Eclipse period without sequestration in Escherichia coli

Identification and characterization of the Escherichia coli envC gene encoding a periplasmic coiled-coil protein with putative peptidase activity

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