mutS:Gene: Difference between revisions
Fixing Blattner deletion strains in alleles table. |
Table edited by Azweifel via TableEdit |
||
| Line 347: | Line 347: | ||
| | | | ||
[[cgscmutation:101976|CGSC:101976]] | [[cgscmutation:101976|CGSC:101976]] | ||
| | |||
|- | |||
| | |||
MutS F596A | |||
| | |||
| | |||
F596A | |||
| | |||
| | |||
* Mildly defective ATPase activity | |||
* Defective MutH activation ''in vitro'' | |||
* Moderately elevated mutation and DNA recombination rates ''in vivo'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS H760A | |||
| | |||
| | |||
H760A | |||
| | |||
| | |||
* Mildly defective ATPase activity | |||
* Defective MutH activation ''in vitro'' | |||
* Moderately elevated mutation and DNA recombination rates ''in vivo'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS H728A | |||
| | |||
| | |||
H728A | |||
| | |||
| | |||
* Mildly defective ATPase activity | |||
* Defective MutH activation ''in vitro'' | |||
* Moderately elevated mutation and DNA recombination rates ''in vivo'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS S668A/T669A | |||
| | |||
| | |||
S668A/T669A | |||
| | |||
| | |||
*Modest reduction of K<sub>cat</sub> (~three-fold) | |||
*Fails to activate MMR | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS D693N | |||
| | |||
| | |||
D693N | |||
| | |||
| | |||
*Modest reduction of K<sub>cat</sub> (~three-fold) | |||
*Fails to activate MMR | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS S668A/T669A/E694A | |||
| | |||
| | |||
S668A/T669A/E694A | |||
| | |||
| | |||
*Defective in DNA binding | |||
*Defective in MMR | |||
*Catalyzes ATP hydrolysis better than single E694A mutant | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS K620M | |||
| | |||
| | |||
K620M | |||
| | |||
| | |||
*Severely reduced ATP binding capacity | |||
*Fails to activate MutH in MMR initiation assays | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS E694Q | |||
| | |||
| | |||
E694Q | |||
| | |||
| | |||
*Binds ATP better than the wt MutS,but hydrolyzes ATP poorly | |||
*Supports low-level MutH activation in a mismatch-independent manner | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS F36A | |||
| | |||
| | |||
F36A | |||
| | |||
| | |||
*Fails to recognize a mismatch site hence failing to initiate MMR | |||
*Loses mismatch binding capacity | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS D693A | |||
| | |||
| | |||
D693A | |||
| | |||
| | |||
*Binds ATP better than the wt MutS,but hydrolyzes ATP poorly | |||
*Supports low-level MutH activation in a mismatch-independent manner | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS E38Q | |||
| | |||
| | |||
E38Q | |||
| | |||
| | |||
*Binds DNA better than wt MutS | |||
*Activates MutH ~50% more than the wt MutS in correlation with increased affinity for heteroduplex DNA | |||
*Completely inactive in MMR and in preventing homologous recombination ''in vivo'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS E694A | |||
| | |||
| | |||
E694A | |||
| | |||
| | |||
*Binds ATP better than the wt MutS,but hydrolyzes ATP poorly | |||
*Supports low-level MutH activation in a mismatch-independent manner | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS E38A | |||
| | |||
| | |||
E38A | |||
| | |||
| | |||
*Exhibits moderately increased affinity for homoduplex DNA ''in vitro'' | |||
*MMR defective ''in vivo'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS E177A | |||
| | |||
| | |||
E177A | |||
| | |||
| | |||
*Unable to form H bonds that link domains I and II | |||
*Indistinguishable from Δ''mutS'' in the ''in vivo'' MMR and recombination assays | |||
*Possesses a lower affinity for heteroduplex DNA ''in vitro'' in the presence of ATP | |||
*Possesses a higher affinity for homoduplex DNA ''in vitro'' in the presence of ATP | |||
*Hyperactive in activating MutH with 2-fold and 4-fold increases observed relative to the wt MutS for heteroduplex and homoduplex DNA, respectively | |||
*Reduced ATP hydrolysis | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS T115A | |||
| | |||
| | |||
T115A | |||
| | |||
| | |||
*Unable to form H bonds that link domains I and II | |||
*Indistinguishable from Δ''mutS'' in the ''in vivo'' MMR and recombination assays | |||
*Possesses a lower affinity for heteroduplex DNA ''in vitro'' in the presence of ATP | |||
*Possesses a higher affinity for homoduplex DNA ''in vitro'' in the presence of ATP | |||
*Hyperactive in activating MutH with 2-fold and 4-fold increases observed relative to the wt MutS for heteroduplex and homoduplex DNA, respectively | |||
*Reduced ATP hydrolysis | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS R197E/R198E | |||
| | |||
| | |||
R197E/R198E | |||
| | |||
| | |||
*Disrupts the domain interface more extensively than the E177A or T115A mutation | |||
*''In vivo'' defects similar to E177A and T115A mutations | |||
*Relatively normal DNA binding | |||
*Slightly elevated affinity for homoduplex DNA in the presence of ATP | |||
*Completely fails to activate MutH ''in vitro'' | |||
| | |||
PMID:12606120 | |||
| | |||
| | |||
|- | |||
| | |||
MutS R197E/R198E/R199E | |||
| | |||
| | |||
R197E/R198E/R199E | |||
| | |||
| | |||
*Disrupts the domain interface more extensively than the E177A or T115A mutation | |||
*''In vivo'' defects similar to E177A and T115A mutations | |||
*Probably results in an unstable protein, which is found in inclusion bodies when over-expressed | |||
| | |||
PMID:12606120 | |||
| | |||
| | | | ||
Revision as of 21:04, 13 April 2011
{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>
| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| Nomenclature | Location(s) and DNA Sequence | Sequence Features | Alleles and Phenotypes | Genetic Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Gene_nomenclature for help with entering information in the Gene Nomenclature table.
| Standard name |
mutS |
|---|---|
| Mnemonic |
Mutator |
| Synonyms |
ECK2728, b2733, JW2703, fdv, ant, plm[1] |
| edit table |
Notes
Location(s) and DNA Sequence
See Help:Gene_location for help entering information in the Gene Location and DNA sequence table.
| Strain | Map location | Genome coordinates | Genome browsers | Sequence links |
|---|---|---|---|---|
|
MG1655 |
61.54 minutes |
MG1655: 2855115..2857676 |
||
|
NC_012967: 2751953..2754514 |
||||
|
NC_012759: 2740927..2743488 |
||||
|
W3110 |
|
W3110: 2855749..2858310 |
||
|
DH10B: 2947657..2950218 |
||||
| edit table |
Notes
Sequence Features
See Help:Gene_sequence_features for help in entering sequence features in EcoliWiki.
| Feature Type | Strain | Genomic Location | Evidence | Reference | Notes |
|---|---|---|---|---|---|
| edit table |
Notes
Alleles and Phenotypes
See Help:Gene_alleles for how to enter or edit alleles and phenotypes in EcoliWiki.
| Allele | Nt change(s) | AA change(s) | Phenotype: Type | Phenotype: Description | Reference | Availability | Comments |
|---|---|---|---|---|---|---|---|
|
ΔmutS (Keio:JW2703) |
deletion |
deletion |
|||||
|
mutS::Tn5KAN-I-SceI (FB20917) |
Insertion at nt 2340 in Minus orientation |
contains pKD46 | |||||
|
mutS::Tn5KAN-I-SceI (FB20918) |
Insertion at nt 2340 in Minus orientation |
does not contain pKD46 | |||||
|
mutS201::Tn5 |
|||||||
|
mutS215::Tn10 |
|||||||
|
mutS3 |
|||||||
|
mutS210 |
|||||||
|
mutS104::mini-Tn10 |
|||||||
|
ΔmutS738::kan |
|||||||
|
MutS F596A |
F596A |
|
|||||
|
MutS H760A |
H760A |
|
|||||
|
MutS H728A |
H728A |
|
|||||
|
MutS S668A/T669A |
S668A/T669A |
|
|||||
|
MutS D693N |
D693N |
|
|||||
|
MutS S668A/T669A/E694A |
S668A/T669A/E694A |
|
|||||
|
MutS K620M |
K620M |
|
|||||
|
MutS E694Q |
E694Q |
|
|||||
|
MutS F36A |
F36A |
|
|||||
|
MutS D693A |
D693A |
|
|||||
|
MutS E38Q |
E38Q |
|
|||||
|
MutS E694A |
E694A |
|
|||||
|
MutS E38A |
E38A |
|
|||||
|
MutS E177A |
E177A |
|
|||||
|
MutS T115A |
T115A |
|
|||||
|
MutS R197E/R198E |
R197E/R198E |
|
|||||
|
MutS R197E/R198E/R199E |
R197E/R198E/R199E |
|
| ||||
| edit table |
Notes
Genetic Resources
See Help:Gene_resources for help entering information into the Genetic Resources table.
| Resource | Resource Type | Source | Notes/Reference |
|---|---|---|---|
|
JW2703 |
Plasmid clone |
Status:Clone OK Primer 1:GCCAGTGCAATAGAAAATTTCGA Primer 2:CCaACCAGGCTCTTCAAGCGATA | |
|
Linked marker |
est. P1 cotransduction: 32% [7] | ||
|
Linked marker |
est. P1 cotransduction: 30% [7] | ||
| edit table |
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
|
| ||
| edit table |
Notes
Links
| Name | URL | Comments |
|---|---|---|
| edit table |
<protect>
References
See Help:References for how to manage references in EcoliWiki.
- ↑ Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 Baba, T et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2 2006.0008 PubMed
- ↑ 3.0 3.1 3.2 CGSC: The Coli Genetics Stock Center
- ↑ 4.0 4.1 Kang, Y et al. (2004) Systematic mutagenesis of the Escherichia coli genome. J. Bacteriol. 186 4921-30 PubMed
- ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 Junop, MS et al. (2003) In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination. DNA Repair (Amst.) 2 387-405 PubMed
- ↑ Kitagawa, M et al. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12 291-9 PubMed
- ↑ 7.0 7.1 The Tn10 insertion sites determined by Nichols et al. 1998 (PMID:9829956) were reannotated by alignment with E. coli K-12 genome sequence (GenBank accession NC_000913). P1 contransduction frequencies were calculated using the formula of Wu (PMID:5338813).