Streptococcus pneumoniae sequence GrpE

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

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C530S825000, C930S010000

Statutory Invention Registration

active

H0002023

ABSTRACT:

BACKGROUND OF THE INVENTION
This invention provides isolated DNA sequences, proteins encoded thereby, and methods of using said DNA and protein in a variety of applications.
Widespread antibiotic resistance in common pathogenic bacterial species has justifiably alarmed the medical and research communities. Frequently, resistant organisms are co-resistant to several antibacterial agents. Penicillin resistance in
Streptococcus pneumoniae
has been particularly problematic. This organism causes upper respiratory tract infections. Modification of a penicillin-binding protein (PBP) underlies resistance to penicillin in the majority of cases. Combating resistance to antibiotic agents will require research into the molecular biology of pathogenic organisms. The goal of such research will be to identify new antibacterial agents.
While researchers continue to develop antibiotics effective against a number of microorganisms,
Streptococcus pneumoniae
has been more refractory. In part, this is because
Streptococcus pneumoniae
is highly recombinogenic and readily takes up exogenous DNA from its surroundings. Thus, there is a need for new antibacterial compounds and new targets for antibacterial therapy in
Streptococcus pneumoniae.


REFERENCES:
Packschies, et al. “GrpE Accelerates Nucleotide Exchange of the Molecular Chaperone DnaK with an Associative Displacement Mechanism.”Biochemistry36 (12) : 3417-3422 (Mar. 25, 1997).
Pierpaoli, et al. “The Power Stroke of the DnaK/DnaJ/GrpE Molecular Chaperone System.”J. Mol. Biol.269 : 757-768 (1997).
Amemura-Maekawa and Watanabe. “Cloning and sequencing of the dnaK and grpE genes ofLegionella pneumophila.”Gene197 : 165-168 (1997).
Pierpaoli, et al. “Control of the DnaK Chaperone Cycle by Substoichiometric Concentrations of the Co-chaperones DnaJ and GrpE.”The Journal of Biological Chemistry273 (12) : 6643-6649 (Mar. 20, 1998).
Jayaraman, et al. “Transcriptional analysis of theStreptococcus mutanshrcA, grpE and dnaK genes and regulation of the expression in the response to heat shock and environmental acidification.”Molecular Microbiology25(2):329-341 (1997).
Wu, et al. “Isolation and Characterization of Point Mutations in theEscherichia coligrpE Heat Shock Gene.”Journal of Bacteriology17 (22):6965-6973 (Nov., 1994).
Harrison, et al. “Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK.”Science276:431-435 (Apr. 18, 1997).
Wu, et al. “Structure-function analysis of theEscherichia coliGrpE heat shock protein.”The EMBO Journal15 (18):4806-4816 (1996).

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