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PMID: 7685908 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Activation of a bacterial lipase by its chaperone.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 12 ·1993-06-15 ·Pages 5682-6

Hobson AH, Buckley CM, Aamand JL, Jørgensen ST, Diderichsen B, McConnell DJ

Abstract

The gene lipA of Pseudomonas cepacia DSM 3959 encodes a prelipase from which a signal peptide is cleaved during secretion, producing a mature extracellular lipase. Expression of lipase in several heterologous hosts depends on the presence of another gene, limA, in cis or in trans. Lipase protein has been overproduced in Escherichia coli in the presence and absence of the lipase modulator gene limA. Therefore, limA is not required for the transcription of lipA or for the translation of the lipA mRNA. However, no lipase activity is observed in the absence of limA. limA has been overexpressed and encodes a 33-kDa protein, Lim. If lipase protein is denatured in 8 M urea and the urea is removed by dialysis, lipase activity is quantitatively recovered provided Lim protein is present during renaturation. Lip and Lim proteins form a complex precipitable either by an anti-lipase or anti-Lim antibody. The Lim protein has therefore the properties of a chaperone.

Related Genes
limA lipA
MeSH Terms
Bacterial Proteins/genetics,metabolism Burkholderia cepacia/enzymology,genetics Cloning, Molecular Enzyme Activation Enzyme Precursors/metabolism Escherichia coli/genetics Gene Expression Genes, Bacterial Genes, Regulator Kinetics Lipase/biosynthesis,genetics,metabolism Plasmids Protein Biosynthesis Protein Sorting Signals/metabolism RNA, Messenger/metabolism Recombinant Proteins/biosynthesis,isolation & purification,metabolism Transcription, Genetic
Chemicals
Bacterial Proteins Enzyme Precursors Protein Sorting Signals RNA, Messenger Recombinant Proteins Lipase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hobson A H
Department of Genetics, Trinity College, Dublin, Ireland.
Buckley C M
Aamand J L
Jørgensen S T
Diderichsen B
McConnell D J
References (30)
30 references, click to expand
  1. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts.
    J Biol Chem. 1965 Sep;240(9):3685-92 PMID: 4284300
  2. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain.
    Proc Natl Acad Sci U S A. 1961 Sep 15;47:1309-14 PMID: 13683522
  3. Assembly of bacterial ribosomes.
    Science. 1973 Mar 2;179(4076):864-73 PMID: 4569247
  4. Assembly of SV40 chromatin in a cell-free system from Xenopus eggs.
    Cell. 1977 Feb;10(2):237-43 PMID: 189936
  5. Functional expression of cloned yeast DNA in Escherichia coli: specific complementation of argininosuccinate lyase (argH) mutations.
    J Mol Biol. 1978 Apr 25;120(4):517-32 PMID: 349166
  6. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA.
    Nature. 1978 Oct 5;275(5679):416-20 PMID: 692721
  7. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
    Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4 PMID: 388439
  8. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes.
    Anal Biochem. 1980 Nov 15;109(1):76-86 PMID: 6258458
  9. Biochemical studies of the human thymocyte cell-surface antigens T6, T9 and T10.
    Cell. 1981 Mar;23(3):771-80 PMID: 7013988
  10. Regulation of a membrane component required for protein secretion in Escherichia coli.
    Cell. 1982 Aug;30(1):311-9 PMID: 6751561
  11. Posttranslational processing of the LDL receptor and its genetic disruption in familial hypercholesterolemia.
    Cell. 1982 Oct;30(3):715-24 PMID: 6291781
  12. Vectors for selective expression of cloned DNAs by T7 RNA polymerase.
    Gene. 1987;56(1):125-35 PMID: 3315856
  13. Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.
    EMBO J. 1987 Nov;6(11):3465-70 PMID: 2828030
  14. A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope.
    J Bacteriol. 1989 May;171(5):2795-802 PMID: 2496115
  15. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli.
    Genes Dev. 1989 Jul;3(7):1035-44 PMID: 2673920
  16. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo.
    Nature. 1989 Oct 5;341(6241):462-4 PMID: 2507926
  17. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold.
    Nature. 1989 Nov 16;342(6247):248-51 PMID: 2478891
  18. An efficient temperature-inducible vector incorporating the T7 gene 10 translation initiation leader region.
    Nucleic Acids Res. 1990 Feb 25;18(4):1070 PMID: 2179865
  19. PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli.
    Cell. 1990 Jun 1;61(5):833-42 PMID: 2111734
  20. Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes.
    J Bacteriol. 1991 Jan;173(2):559-67 PMID: 1987151
  21. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex.
    Nature. 1991 Jun 6;351(6326):491-4 PMID: 2046751
  22. The Escherichia coli groE chaperonins.
    Semin Cell Biol. 1990 Feb;1(1):19-25 PMID: 1983267
  23. Molecular chaperones.
    Annu Rev Biochem. 1991;60:321-47 PMID: 1679318
  24. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.
    Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9330-4 PMID: 1924396
  25. A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export.
    Mol Microbiol. 1991 May;5(5):1273-83 PMID: 1956302
  26. Cloning, nucleotide sequencing, and expression in Escherichia coli of a lipase and its activator genes from Pseudomonas sp. KWI-56.
    Agric Biol Chem. 1991 Sep;55(9):2349-57 PMID: 1368739
  27. Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected].
    Mol Microbiol. 1991 Jun;5(6):1507-10 PMID: 1686294
  28. Purification, molecular cloning, and expression of lipase from Pseudomonas aeruginosa.
    Arch Biochem Biophys. 1992 Aug 1;296(2):505-13 PMID: 1632642
  29. Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1.
    J Gen Microbiol. 1992 Jul;138(7):1325-35 PMID: 1512563
  30. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.12.5682
Published
1993-06-15
Pages
5682-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC46785
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.90.12.5682 PMC Full Text View journal details
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