1887

Abstract

A gene with homology to those encoding an unusual class of C-terminal processing proteases that flanks the invasion-associated locus of has been identified. The 1302 bp gene, termed is located immediately upstream of the gene and encodes a predicted nascent product of 434 amino acids, producing a mature protein of 411 amino acid residues. The CtpA appears to undergo autolysis producing multiple products of 43-46 kDa, and a second group of products of 36-37 kDa. Production of CtpA gives a single product of 41.8 kDa. In addition to a computer-predicted N-terminal secretory signal sequence, the molecular mass difference versus indicates that CtpA is likely to be secreted and post-translationally modified. The full-length CtpA protein shows 30% identity to the CtpA protein of sp. 6803 (69% overall sequence similarity). The mature CtpA protein also has significant homology to the tail-specific protease (Tsp) of with 22% identity and 62% similarity to an internal region of the 660 amino acid Tsp. The CtpA protein does not appear to exhibit haemolysin, collagenase, or caseinase activity. The gene is conserved in all species examined, as determined by hybridization analyses, but it was not found in or The gene does not directly affect the erythrocyte-invasion phenotype conferred by but its homology to other stress-response processing proteases implies an important role in survival of this intracellular pathogen.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-143-4-1221
1997-04-01
2024-12-03
Loading full text...

Full text loading...

/deliver/fulltext/micro/143/4/mic-143-4-1221.html?itemId=/content/journal/micro/10.1099/00221287-143-4-1221&mimeType=html&fmt=ahah

References

  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. 1990; Basic local alignment search tool.. J Mol Biol 215:403–410
    [Google Scholar]
  2. Anbudurai P. R., Tsafrir S. M., Ohad I., Shestakov S.V., Pakrasi H. B. 1994; The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex.. Proc Natl Acad Sci USA 91:8082–8086
    [Google Scholar]
  3. Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Pakrasi H. B., Seidman J. G., Smith J. A., Strahl K. 1995; Current Protocols in Molecular Biology.. New York: John Wiley
    [Google Scholar]
  4. Barber J., Anderson B. 1992; Too much of a good thing: light can be bad for photosynthesis. Trends Biochem Sci 17:61–66
    [Google Scholar]
  5. Bäumler A. J., Kuste J. G., Stojiljkovic I., Heffron F. 1994; Salmonella typhimurium loci involved in survival within macrophages.. lnfect lmmun 62:1623–1630
    [Google Scholar]
  6. Bowyer J. R., Packer J. C., McCormack B. A., Whitelegge J. P., Robinson C., Taylor M. A. 1992; Carboxyl-terminal processing of the D1 protein and photoactivation of water-splitting in Photosystem 11.. J Biol Chem 267:5424–5433
    [Google Scholar]
  7. Boyer H. W., Roulland-Dussoix D. 1969; A complementation analysis of the restriction and modification of DNA in Escherichia coli.. J Mol Bio 41:459–472
    [Google Scholar]
  8. Brenner D. J., O'Connor S. P., Hollis D. G., Weaver R. E., Steigerwalt A. G. 1991; Molecular characterization and proposal of a neotype strain for Bartonella bacilliformis.. J Clin Microbiol 29:1299–1302
    [Google Scholar]
  9. Chung C. T., Niemela S. L., Miller R. H. 1989; A One-step preparation of competent Escherichia coli : transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86:2172–2175
    [Google Scholar]
  10. Churin Y. N., Shalak 1. N., Borner T., Shestakov S. V. 1995; Physical and genetic map of the chromosome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol 177:3337–3343
    [Google Scholar]
  11. Daly J. S., Worthington M. G., Brenner D. J., Moss C. W., Hollis D. G., Weyant R. S., Steigerwalt A. G., Weaver R. E., Daneshvar M. 1., O'Connor S. P. 1993; Rochalimaea elizabethae sp. nov. isolated from a patient with endocarditis. J Clin Microbiol 31:872–881
    [Google Scholar]
  12. Falkow S. 1996; The evolution of pathogenicity in Escherichia, Shigella, and Salmonella. In Escherichia coli and Salmonella : Cellular and Molecular Biology, 2nd edn.,. 2723–2729 Edited by F. C. Neidhardt and others. Washington, DC: American Society for Microbiology..
    [Google Scholar]
  13. Feinberg A. P., Vogelstein B. 1984; A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. . Anal Biochem 137:266–267
    [Google Scholar]
  14. Gold L., Pribnow D., Schneider T., Shinedling S., Singer B., Stormo G. 1981; Translation initiation in prokaryotes.. Annu Rev Microbio 35:365–407
    [Google Scholar]
  15. Hara H., Yamamoto Y., Higashitani A., Suzuk H., Nishimura Y. 1991; Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in the C-terminal processing of penicillin-binding protein 3.. J Bacteriol 173:4799–4813
    [Google Scholar]
  16. Herrin D. L., Schmidt G. W. 1988; Rapid, reversible staining of Northern blots prior to hybridization.. Biotechniques 6:196–200
    [Google Scholar]
  17. Hofmann K., Baron M. D. 1996; BOXSHADE : 3.2. Lausanne, Switzerland : http ://ulrec3.unil.ch/software/BOX_form. html .
    [Google Scholar]
  18. Keiler K. C., Sauer R. T. 1995; Identification of active site residues of the Tsp protease.. J Biol Chem 270:28864–28868
    [Google Scholar]
  19. Keiler K. C., Sauer R. T. 1996; Sequence determinants of Cterminal substrate recognition by the Tsp protease.. J Biol Chem 271:2589–2593
    [Google Scholar]
  20. Keiler K. C., Silber K. R., Downard K. M., Papayannopoulos 1. A., Biemann A., Sauer R. T. 1995; C-terminal specific protein degradation : activity and substrate specificity of the Tsp protease.. Protein Sci 4:1507–1515
    [Google Scholar]
  21. Keiler K. C., Waller P. R. H., Sauer R. T. 1996; Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA.. Science 271:990–993
    [Google Scholar]
  22. Kordick D. L., Breitschwerdt E.B. 1995; Intraerythrocytic presence of Bartonella henselae.. J Clin Microbio 33:1655–1656
    [Google Scholar]
  23. Laemmli U. K. 1970; Cleavage of stuctural proteins during the assembly of the head of bacteriophage T4.. Nature 227:680–685
    [Google Scholar]
  24. Landick R., Turnbough C. L.Jr, Yanofsky C. 1996; Transcription attenuation. In Escherichia coli and Salmonella : Cellular and Molecular Biology, 2nd edn.,. 1263–1286 Edited by F. C. Neidhardt and others. Washington, DC : American Society for Microbiology.
    [Google Scholar]
  25. McLure W. R. 1985; Mechanism and control of transcription initiation in prokaryotes.. Annu Rev Biochern 54:171–204
    [Google Scholar]
  26. Meinkoth J., Wahl G. 1984; Hybridization of nucleic acids immobilized on solid supports.. Anal Biochem 138:267–284
    [Google Scholar]
  27. Miller C. G. 1996; Protein degradation and proteolytic modification. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn,. 938–954 Edited by F. C. Neidhardt and others. Washington, DC : American Society for Microbiology. .
    [Google Scholar]
  28. Minnick M. F., Heinzen R. A., Frazier M. E., Mallavia L. P. 1990; )Characterization and expression of the c66E’ gene of Coxiella burnetii.. J Gen Microbiol 138:1099–1107
    [Google Scholar]
  29. Mitchell S. J, Minnick M. F. 1995; Characterization of a twogene locus from Bartonella bacilliformis associated with the ability to invade human erythrocytes. Infect Immun 63:1552–1562
    [Google Scholar]
  30. Myers W. F., Wisseman C. L.Jr, Fiset P., Oaks E. V., Smith J. F. 1979; Taxonomic relationship of vole agent to Rochalimaea guintana.. Infect lmmun 26:976–983
    [Google Scholar]
  31. Nixon P. J., Trost J. T., Diner B. A. 1992; Characterization of a novel Rochalimaea species, R. henselae sp. nov., isolated from blood of a febrile, human immunodeficiency virus-positive patient.. J Clin Microbio 30:265–274
    [Google Scholar]
  32. Pearson W. R. 1990; Rapid and sensitive sequence comparison with FASTP and FASTA.. Methods Enzymol 183:63–98
    [Google Scholar]
  33. Regnery R., Tappero J. 1995; Unraveling mysteries associated with cat-scratch disease, bacillary angiomatosis, and related syndromes. . Emerg lnfect Dis 1:16–20
    [Google Scholar]
  34. Reynafarje C., Ramos J. 1961; The hemolytic anemia of human Bartonellosis. . Blood 17:562–578
    [Google Scholar]
  35. Rosenberg M., Court D. 1979; Regulatory sequences involved in the promotion and termination of RNA transcription . Annu Rev Genet 13:319–353
    [Google Scholar]
  36. Sancar A., Hack A. M., Rupp W. D. 1979; RSimple method for identification of plasmid-coded proteins.. J Bacteriol 137:692
    [Google Scholar]
  37. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. . Proc Natl Acad Sci USA 74:5463–5467
    [Google Scholar]
  38. Shestakov S. V., Anbudurai P. R., Stanbekovas G. E., Gadzhiev A., Lind L. K., Pakrasi H. B. 1994; Molecular cloning andcharacterization of the ctpA gene encoding a carboxyl-terminal processing protease.. J Biol Chem 269:19354–19359
    [Google Scholar]
  39. Silber K. R., Keiler K. C., Sauer R. T. 1992; Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. . Proc Natl Acad Sci USA 89:295–299
    [Google Scholar]
  40. Southern E. M. 1975; Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Bio 98:503–517
    [Google Scholar]
  41. Stormo D. G., Schneide T. D., Gold L., Ehrenfeuch A. 1982; Use of the ‘ perceptron ’ algorithm to distinguish translational initiation sites in E. coli.. Nucleic Acids Res 10:2997–3011
    [Google Scholar]
  42. Taguchi F., Tamamoto Y., Satoh K. 1995; Recognition of the structure around the site of cleavage by the carboxyl-terminal processing protease for the D1 precursor protein of the photosystem II reaction center. J Biol Chem 270:10711–10716
    [Google Scholar]
  43. Takahash M., Shiraishi T., Asada K. 1988; COOH-terminal residues of D1 and the 44 kDa CPa-2 at spinach photosystem II core complex. . FEBS Lett 240: 6–8
    [Google Scholar]
  44. Thompson J. D., Higgins D. G., Gibson T. J. 1994; CLUSTAL w: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice. . Nucleic Acids Res 22:4673–4680
    [Google Scholar]
  45. Vinson A. P., Fuller H. S. 1961; Studies on trench fever. I. Propagation of rickettsia-like microorganisms from a patient’s blood.. Pathol Microbiol152–166s
    [Google Scholar]
  46. Von-Heijne G. 1986; A new method for predicting signal sequence cleavage sites.. Nucleic Acids Res 14:4683–4690
    [Google Scholar]
  47. Weiss E., Dasch G. A. 1982; Differential characteristics of strains of Rochalimaea : Rochalimaea vinsonii sp. nov., the Canadian Vole Agent.. lnt J Syst Bacteriol 32:305–314
    [Google Scholar]
  48. Yanisch-Perron C., Vieira J., Messing J. 1985; Improved M13 phage cloning vectors and host strains : nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103–119
    [Google Scholar]
  49. Young R. A., Davis R. W. 1983; Yeast RNA polymerase II genes : isolation with antibody probes.. Science 222:778–782
    [Google Scholar]
/content/journal/micro/10.1099/00221287-143-4-1221
Loading
/content/journal/micro/10.1099/00221287-143-4-1221
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error