hfq:Gene

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Nomenclature Location(s) and DNA Sequence Sequence Features Alleles and Phenotypes Genetic Interactions Genetic Resources Accessions Links References Suggestions

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Nomenclature

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Standard name

hfq

Mnemonic

Host factor for Q beta

Synonyms

ECK4168, b4172, JW4130, HF-I, HF-1[1][2]

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Notes

Location(s) and DNA Sequence

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Strain Map location Genome coordinates Genome browsers Sequence links

MG1655

94.8 minutes 

MG1655: 4398311..4398619
<gbrowseImage> name=NC_000913:4398311..4398619 source=MG1655 preset=GeneLocation </gbrowseImage>

REL606

NC_012967: 4378443..4378751
<gbrowseImage> name=NC_012967:4378443..4378751 source=REL606 preset=GeneLocation </gbrowseImage>

BW2952

NC_012759: 4337046..4337354
<gbrowseImage> name=NC_012759:4337046..4337354 source=BW2952 preset=GeneLocation </gbrowseImage>

W3110

 

W3110: 4404968..4405276
<gbrowseImage> name=NC_007779:4404968..4405276 source=W3110 preset=GeneLocation </gbrowseImage>

DH10B

DH10B: 4498673..4498981
<gbrowseImage> name=NC_010473:4498673..4498981 source=DH10B preset=GeneLocation </gbrowseImage>

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Notes

Sequence Features

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See Help:Gene_sequence_features for help in entering sequence features in EcoliWiki.

Feature Type Strain Genomic Location Evidence Reference Notes

Coding Start (SO:0000323)

MG1655

4398314

Edman degradation

PMID:805130[3]
PMID:2020545[4]
PMID:8809757[5]
PMID:9245691[6]


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Notes

Alleles and Phenotypes

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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

hfq(del) (Keio:JW4130)

deletion

deletion

PMID:16738554[7]

Shigen
CGSC10973[8]

hfq-722(del)::kan

PMID:16738554[7]

CGSC:101354

hfq2::omega

Insertion of omega cassette near the end of hfq sequence

Growth Phenotype

hfq maintained limited if not full activity

PMID:7984093[9]

the resulting phenotypes showed no substantial difference from hfq+ parent

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

Cell Shape

Elongated Cells(Fig 3).

PMID:7984093[9]

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

Growth Phenotype

Decreased growth and yield (table 2).

PMID:7984093[9]

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

Cell Shape

Relaxed coiling (Fig. 4)

PMID:7984093[9]

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

Sensitivity to

Increased sensitivity to Ultraviolet (u.v.) light

PMID:7984093[9]

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

Growth Phenotype

spontaneous mutagenesis

PMID:7984093[9]

hfq1

Growth Phenotype

stabilizes ompA mRNA

PMID:9826663[10]

disruption of hfq1 results in an increase of ompA mRNA half-life but does not affect the level of degradosomal components

hfq1::omega

Insertion of omega cassette near the start of hfq sequence

oxidation

Increased oxidation of various carbon sources (Fig. 5).

PMID:7984093[9]

Hfq-Q8A

Glutamine to Alanine at postion 8

suppression

Hfq binding protein regulates mRNA translation by binding to OxyS to repress rpoS mRNA translation. Proximal surface mutation exhibit a 2.3 to 3.2-fold decrease in affinity to rpoS compared to wildtype Hfq, table 1.

PMID:21889623[11]

Hfq-R16A

Argenine to Alanine at position 16.

suppression

Proximal surface mutation exhibit a 2.3 to 3.2-fold decrease in affinity to DsrA compared to wildtype Hfq. Thus translation cannot continue, table 1.

PMID:21889623[11]

Hfq-F39A

Phenylalanine to alanine at position 39

suppression

Proximal surface mutation exhibit a 2.3 to 3.2-fold decrease in affinity to DsrA compared to wildtype Hfq. Thus translation cannot continue, table 1.

PMID:21889623[11]

hfq1::omega

A disruption in the middle of the hfq gene

Change in gene expression

strongly reduced sigma levels during entry into stationary phase

PMID:8654929[12]

Error in labeling see Figure 2

hfq1::omega

A disruption in the middle of the hfq gene

A change in gene expression

the translation of rpoS::lacZ is disrupted in the mutant strain.

PMID:8654929[12]

See Figure 3

hfq1::omega

A disruption in the middle of the hfq gene

A change in gene expression

Despite any increase in osmotic upshift there is no increase in cellular sigma content.

PMID:8654929[12]

Error in labeling see Figure 1

hfq::omega

A disruption in the middle of the hfq gene

A change in gene expression

osmotic induction of the translational rpoS742::lacZ fusion is impaired.

PMID:8654929[12]

See figure 4

F42A

Phenylalanine to alanine at position 42

suppression

Mutation causes a decrease in biding affinity to rpsO, table 1.

PMID:21889623[11]

hfq::omega

A disruption in the middle of hfq gene

A change in gene expression

Residual amounts of sigma in exhibit normal regulation

PMID:8654929[12]

See Figure 6

hfq(del)

Null mutation

Change in the expression of a gene

Overexpression of rybB in both the exponential and stationary growth phase.

PMID:17416652[13]

See Figure 5 C.

hfq772(del)::FRT

Deletion

Mutagenesis Rate

Decrease in stress induced mutagenesis (SIM).

PMID:23224554[14]

The mutation conferred a strong decrease in SIM, the mutant frequency was reduced by over 90 % of the wild type levels. See table S3 for full experimental data.

hfq772(del)::FRT

Deletion

Sensitivity to

Increase UV sensitivity

PMID:23224554[14]

The mutation conferred an increase in sensitivity toward UV. See tables S7 and S1 for summarized results.

hfq772(del)::FRT

Deletion

Sensitivity to

Increase sensitivity toward SDS-EDTA

PMID:23224554[14]

The mutation conferred an increase in SDS-EDTA sensitivity. See table S7 and S1 for summarized results.

SMR4562 yiaG-yfp FRTcatFRT hfq722(del)::FRTKanFRT

Deletion

SigmaS activity

Decrease in Sigma S activity

PMID:23224554[14]

Parental Strain: SMR10582 Experimental Strain: SMR14295

See table S8 for full experimental results.

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Notes

Genetic Interactions

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Interactor Interaction Allele Score(s) Reference(s) Accessions Notes

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Notes

Genetic Resources

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See Help:Gene_resources for help entering information into the Genetic Resources table.

Resource Resource Type Source Notes/Reference

JW4130

Plasmid clone

Shigen

PMID:16769691[15]

Status:Clone OK

Primer 1:GCCGCTAAGGGGCAATCTTTACA

Primer 2:CCTTCGGTTTCTTCGCTGTCCTG

3A1

Kohara Phage

Genobase

PMID:3038334[16]

cadB2231::Tn10

Linked marker

CAG18488 = CGSC7479[8]

est. P1 cotransduction: 17% [17]
Synonyms:zjd-2231::Tn10

cycA30::Tn10

Linked marker

CAG12073 = CGSC7482[8]

est. P1 cotransduction: 34% [17]

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc

EcoCyc:EG10438

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10438

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000431

Escherichia coli str. K-12 substr. MG1655

NCBI (EcoliWiki Page)

GeneID:948689

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0433

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0013659

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. Carmichael, GG et al. (1975) The host factor required for RNA phage Qbeta RNA replication in vitro. Intracellular location, quantitation, and purification by polyadenylate-cellulose chromatography. J. Biol. Chem. 250 3607-612 PubMed
  4. Kajitani, M & Ishihama, A (1991) Identification and sequence determination of the host factor gene for bacteriophage Q beta. Nucleic Acids Res. 19 1063-6 PubMed
  5. Green, J et al. (1996) The ndh-binding protein (Nbp) regulates the ndh gene of Escherichia coli in response to growth phase and is identical to Fis. Mol. Microbiol. 20 1043-55 PubMed
  6. Takada, A et al. (1997) DNA binding properties of the hfq gene product of Escherichia coli. Biochem. Biophys. Res. Commun. 236 576-9 PubMed
  7. 7.0 7.1 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
  8. 8.0 8.1 8.2 CGSC: The Coli Genetics Stock Center
  9. 9.0 9.1 9.2 9.3 9.4 9.5 9.6 Tsui, HC et al. (1994) Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. Mol. Microbiol. 13 35-49 PubMed
  10. Vytvytska, O et al. (1998) Host factor I, Hfq, binds to Escherichia coli ompA mRNA in a growth rate-dependent fashion and regulates its stability. Proc. Natl. Acad. Sci. U.S.A. 95 14118-23 PubMed
  11. 11.0 11.1 11.2 11.3 Updegrove, TB & Wartell, RM (2011) The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation. Biochim. Biophys. Acta 1809 532-40 PubMed
  12. 12.0 12.1 12.2 12.3 12.4 Muffler, A et al. (1996) The RNA-binding protein HF-I, known as a host factor for phage Qbeta RNA replication, is essential for rpoS translation in Escherichia coli. Genes Dev. 10 1143-51 PubMed
  13. Thompson, KM et al. (2007) SigmaE regulates and is regulated by a small RNA in Escherichia coli. J. Bacteriol. 189 4243-56 PubMed
  14. 14.0 14.1 14.2 14.3 Al Mamun, AA et al. (2012) Identity and function of a large gene network underlying mutagenic repair of DNA breaks. Science 338 1344-8 PubMed
  15. 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
  16. Kohara, Y et al. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50 495-508 PubMed
  17. 17.0 17.1 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).

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