trpR:Gene Product(s): Difference between revisions

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''trpR55'' is synonymous with ''trpR2'' as studied by Yanofsky, et al, in 1984. <ref>http://cgsc2.biology.yale.edu/Mutation.php?ID=4525</ref>
''trpR55'' is synonymous with ''trpR2'' as studied by Yanofsky, et al, in 1984. <ref>http://cgsc2.biology.yale.edu/Mutation.php?ID=4525</ref>
''trpR2'' acts as a frameshift mutation within the ''trp'' repressor.  As a result, the repressor remains inactive and is unable to bind to the operator of the ''trp'' operon, allowing transcription on the trp operon to proceed with tryptophan synthesis, instead of inhibiting production as it normally would in high levels of tryptophan. 
''trpR2'' does not target a specific functional repressor, since levels of ''trp'' enzymes in strains with ''trpR2'' mutations do not differ from levels found within strains undergoing ''trpR'' amber and ''trpR'' deletion mutations.  <ref name='PMID:6233264'/>


==Localization==
==Localization==

Revision as of 17:24, 8 November 2007

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

TrpR product

Synonyms

DNA-binding transcriptional repressor, tryptophan-binding product[1], B4393 product[2][1], RtrY product[2][1], TrpR product[2][1], regulator for trp operon and aroH; trp aporepressor product[2][1]

Product description

TrpR[2][3];

Component of ; TrpR transcriptional repressor[2][3]; TrpR-Tryptophan transcriptional repressor[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0006350

transcription

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0016564

transcription repressor activity

F

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0000162

tryptophan biosynthetic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

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Interactions

Partner Type Partner Notes

Protein

Subunits of TrpR transcriptional repressor

could be indirect

Protein

Subunits of TrpR-Tryptophan transcriptional repressor

could be indirect

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Notes

trpR55 is synonymous with trpR2 as studied by Yanofsky, et al, in 1984. [4]

trpR2 acts as a frameshift mutation within the trp repressor. As a result, the repressor remains inactive and is unable to bind to the operator of the trp operon, allowing transcription on the trp operon to proceed with tryptophan synthesis, instead of inhibiting production as it normally would in high levels of tryptophan.

trpR2 does not target a specific functional repressor, since levels of trp enzymes in strains with trpR2 mutations do not differ from levels found within strains undergoing trpR amber and trpR deletion mutations. [5]

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MAQQSPYSAA MAEQRHQEWL RFVDLLKNAY QNDLHLPLLN LMLTPDEREA LGTRVRIVEE
LLRGEMSQRE LKNELGAGIA TITRGSNSLK AAPVELRQWL EEVLLKSD
Mol. Wt

12.36 kDa (calc) [2]

pI

5.39[2]

Extinction coefficient

13980 (calc based on 2 Y, 2 W, and 0 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structure Type Organism Accession Residues covered Notes

X-RAY DIFFRACTION

Escherichia coli

1TRO CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION

NMR, 15 STRUCTURES

Escherichia coli

1RCS NMR STUDY OF TRP REPRESSOR-OPERATOR DNA COMPLEX

X-RAY DIFFRACTION

Escherichia coli

1MI7 Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol

NMR, 15 STRUCTURES

Escherichia coli

1CO0 NMR STUDY OF TRP REPRESSOR-MTR OPERATOR DNA COMPLEX

X-RAY DIFFRACTION

Escherichia coli

1P6Z E. Coli Trp Apo-Repressor, Monoclinic Crystal Form

X-RAY DIFFRACTION

Escherichia coli

3WRP FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

2WRP

NMR, 15 STRUCTURES

Escherichia coli

1WRT NMR STUDY OF APO TRP REPRESSOR

NMR, 15 STRUCTURES

Escherichia coli

1WRS NMR STUDY OF HOLO TRP REPRESSOR

X-RAY DIFFRACTION

Escherichia coli

1WRP FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

X-RAY DIFFRACTION

Escherichia coli

1TRR TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX

X-RAY DIFFRACTION

Escherichia coli

1JHG TRP REPRESSOR MUTANT V58I

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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:PD00423

UniProt (EcoliWiki Page)

UniProt:P0A881

PFAM (EcoliWiki Page)

PFAM:PF01371

RefSeq (EcoliWiki Page)

RefSeq:NP_418810

PDB (EcoliWiki Page)

PDB:1JHG

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Notes

Links

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Name URL Comments
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References

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  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ http://cgsc2.biology.yale.edu/Mutation.php?ID=4525
  5. ↑ Yanofsky, C et al. (1984) Repression is relieved before attenuation in the trp operon of Escherichia coli as tryptophan starvation becomes increasingly severe. J. Bacteriol. 158 1018-24 PubMed


Categories

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