Difference between revisions of "PMID:4887874"
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==Main Points of the Paper == | ==Main Points of the Paper == | ||
*π, a new site of initiation of protein synthesis is described | *π, a new site of initiation of protein synthesis is described | ||
− | **operates efficiently to restore permease and acetylase activity to a high level | + | **operates efficiently to restore permease and acetylase activity to a high level when induced |
+ | **regulation/induction is still required, so the authors deduce that π is a new site of translation initiation ( | ||
+ | **not a new site of transcriptional initiation because acetylase is not present in the absence of inducer | ||
== Materials and Methods Used == | == Materials and Methods Used == |
Revision as of 17:13, 15 December 2010
Citation |
Grodzicker, T and Zipser, D (1968) A mutation which creates a new site for the re-initiation of polypeptide synthesis in the z gene of the lac operon of Escherichia coli.J. Mol. Biol. 38:305-14 |
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Abstract |
No abstract in PubMed |
Links | |
Keywords |
Acyltransferases; Chromosome Mapping; Escherichia coli; Genes; Membrane Transport Proteins; Mutation; Operon |
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Main Points of the Paper
- π, a new site of initiation of protein synthesis is described
- operates efficiently to restore permease and acetylase activity to a high level when induced
- regulation/induction is still required, so the authors deduce that π is a new site of translation initiation (
- not a new site of transcriptional initiation because acetylase is not present in the absence of inducer
Materials and Methods Used
- Parent Strain: NG545 (trp-8, SmS Hfr)
- Strain: CA77B (Δlac, trp-8, SmR F-)
- Strain: X103B (Δlac pro, trp-8, SmR F-)
- Strain: M107 (Δlac, suI+, SmR F-)
- Strain: ΔLacW (Δlac, his-, SmR F-)
- Strain: E29 (lac+ , F'/lac+, threonine-, leucine-, B1-, SmR)
- Acetylase assay
- β-galactosidase assay
Phenotype Annotations
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<protect>
Species | Taxon ID | Strain | Gene (if known) | OMP | Phenotype | Details | Evidence | Notes |
---|---|---|---|---|---|---|---|---|
Escherichia coli |
NCBI:562 |
NG545-pi(1)a |
lacZ |
able to metabolize melibiose |
Growth |
growth on melibiose- polar effects |
Plating Assay |
Table 2 |
Escherichia coli |
NCBI:562 |
NG545-pi(1) |
lacZ |
Growth |
able to metabolize lactose only in a suI+ background |
Plating Assay |
Table 2- UAG polar mutation | |
Escherichia coli |
NCBI:562 |
NG545-pi(1)b |
lacZ |
unable to metabolize melibiose |
Growth |
growth on melibiose-polar effects |
Plating Assay |
Table 2- |
Escherichia coli |
NCBI:562 |
NG545-pi(1)a |
lacZ |
reduced beta-galactosidase activity |
Metabolic Activity |
trace amounts when induced |
Biochemical Assay |
Table 2 |
Escherichia coli |
NCBI:562 |
NG545-pi(1)b |
lacZ |
reduced beta-galactosidase activity |
Metabolic Activity |
trace amounts when induced |
Biochemical Assay |
Table 2 |
Escherichia coli |
NCBI:562 |
NG545B |
lacZ |
reduced acetylase activity |
Metabolic Activity |
4.2% of the wild type level when induced |
Biochemical Assay |
Tables 3 and 4 |
Escherichia coli |
NCBI:562 |
NG545-pi(1)aB |
lacZ |
reduced acetylase activity |
Metabolic Activity |
35% of the wild type level when induced |
Biochemical Assay |
Tables 3 and 4 |
Escherichia coli |
NCBI:562 |
NG545-pi(1)bB |
lacZ |
reduced acetylase activity |
Metabolic Activity |
33.5% of the wild type level when induced |
Biochemical Assay |
Tables 3 and 4 |
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</protect>
Notes
References
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