Transcriptional repressor CopR: The structured acidic C terminus is important for protein stability

Journal of Molecular Biology

Volumn 300, Issue 5, 2000, Pages 1021-1031

  Kuhn, Kornelia ^a   Steinmetzer, Katrin ^a   Brantl, Sabine ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

Gram positive bacteria; Plasmid copy number control; Protein stability; Transcriptional repressor

Indexed keywords

DNA BINDING PROTEIN; MUTANT PROTEIN; PROTEIN COPR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; DNA BINDING; HALF LIFE TIME; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

EID: 0034725552     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3929     Document Type: Article

References (31)

1. Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and β-sheet DNA binding proteins
2. Synthesis and beta-conformation of copolypeptides with alternating hydrophilic and hydrophobic residues
3. Molecular analysis of the replication region of the conjugative Streptococcus agalactiae plasmid pIP501 in Bacillus subtilis. Comparison with plasmids pAMβ1 and pSM19035
4. Copy-number control of the streptococcal plasmid pIP501 occurs at three levels
5. RepR protein expression on plasmid pIP501 is controlled by an antisense RNA-mediated transcription attenuation mechanism
6. The copR gene product of plasmid pIP501 acts as a transcriptional repressor at the essential repR promoter
7. An unusually long-lived antisense RNA in plasmid copy-number control: In vivo RNAs encoded by the streptococcal plasmid pIP501
8. Antisense-RNA mediated transcriptional attenuation occurs faster than stable antisense/target RNA pairing: An in vitro study of plasmid pIP501
9. Dual function of the copR gene product of plasmid pIP501
10. Gene organization of the Streptococcus pyogenes plasmid pDB101: Sequence analysis of the orfη-copS region
11. The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator
12. Plasmid copy-number control and better-than-random segregation genes of pSM19035 share a common regulator
13. The pAMβ1 Cop repressor regulates plasmid copy number by controlling transcription of the repE gene
14. Expression of a copy-number control gene (copB) of plasmid R1 is constitutive and growth rate dependent
15. The role of internal packing interactions in determining the structure and stability of a protein
16. P22 Arc repressor: Enhanced expression of unstable mutants by addition of polar C-terminal sequences
17. Protein stability effects of a complete set of alanine substitutions in Arc repressor
18. The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
19. Carboxy-terminal determinants of intracellular protein degradation
20. Purification and characterization of the CopB replication control protein, and precise mapping of its target site in the R1 plasmid
21. DNA sequencing with chain-terminating inhibitors
22. Plasmid pLS1-encoded RepA protein regulates transcription from repAB promoter by binding to a DNA sequence containing a 13-base-pair symmetric element
23. A self-consistent method for the analysis of protein secondary structure from circular dichroism
24. Poly(pro)II helices in globular proteins: Identification and circular dichroic analysis
25. Plasmid pIP501 encoded transcriptional repressor CopR binds asymmetrically at two consecutive major grooves of the DNA
26. Plasmid pIP501 encoded transcriptional repressor CopR binds to its target DNA as a dimer
27. Transcriptional repressor CopR: Structure model based localization of the DNA binding motif
28. Transcriptional repressor CopR: Amino acids involved in forming the dimeric interphase
29. Physical characterisation of the replication region of the Streptococcus faecalis plasmid pAMβ1
30. Control of ColE1 plasmid replication. Interaction of Rom protein with an unstable complex formed by RNAI and RNAII