Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Regulatory functions of the lambda repressor reside in the amino-terminal domain.

Literature DB >> 16068162

Regulatory functions of the lambda repressor reside in the amino-terminal domain.

R T Sauer, C O Pabo, B J Meyer, M Ptashne, K C Backman.

Abstract

The repressor of bacteriophage lambda is a protein containing two domains of approximately equal size. Fragments containing the amino-terminal domain of repressor bind specifically to lambda operator DNA and mediate positive and negative control of lambda transcription both in vitro and in vivo.

Entities: Gene Species

Year: 1979 PMID： 16068162 DOI： 10.1038/279396a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

Keyword Cloud
Cited

42 in total

1. pH-dependent autocleavage of lambda repressor occurs in the operator-bound form: characterization of lambda repressor autocleavage.

Authors: Kaushik Ghosh; Atasi Pal; Rajagopal Chattopadhyaya
Journal: Biochem J Date: 2004-04-15 Impact factor: 3.857

2. How different DNA sequences are recognized by a DNA-binding protein: effects of partial proteolysis.

Authors: P C Supakar; X Y Zhang; S Githens; R Khan; K C Ehrlich; M Ehrlich
Journal: Nucleic Acids Res Date: 1989-11-11 Impact factor: 16.971

3. Structural analysis of the carboxy terminus of bacteriophage lambda repressor determined by antipeptide antibodies.

Authors: R Sussman; H B Alexander
Journal: J Bacteriol Date: 1989-03 Impact factor: 3.490

4. Protein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed Mutagenesis.

Authors: M A Weiss; R Stearman; A Jeitler-Nilsson; M Karplus; R T Sauer
Journal: Biophys J Date: 1986-01 Impact factor: 4.033

9. Interactions among the bHLH domains of the proteins encoded by the Enhancer of split and achaete-scute gene complexes of Drosophila.

Authors: F Gigliani; F Longo; L Gaddini; P A Battaglia
Journal: Mol Gen Genet Date: 1996-07-26

10. Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segments.

Authors: A L Donner; P A Carlson; G B Koudelka
Journal: J Bacteriol Date: 1997-02 Impact factor: 3.490

Regulatory functions of the lambda repressor reside in the amino-terminal domain.

1. pH-dependent autocleavage of lambda repressor occurs in the operator-bound form: characterization of lambda repressor autocleavage.

2. How different DNA sequences are recognized by a DNA-binding protein: effects of partial proteolysis.

3. Structural analysis of the carboxy terminus of bacteriophage lambda repressor determined by antipeptide antibodies.

4. Protein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed Mutagenesis.

5. Quantitative transcription factor binding kinetics at the single-molecule level.

Review 6. The chemistry of regulation of genes and other things.

7. Mutagenic dissection of the sequence determinants of protein folding, recognition, and machine function.

8. How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.

9. Interactions among the bHLH domains of the proteins encoded by the Enhancer of split and achaete-scute gene complexes of Drosophila.

10. Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segments.