1887

Abstract

Temperature-dependent phosphorylation and dephosphorylation of membrane proteins was studied in a number of psychrotrophic Antarctic bacteria which grow between 0 and 30°C. One of them, a isolate, was studied in detail and was found to have three membrane proteins of molecular mass 30, 65 and 85 kDa which were phosphorylated differently in response to low and high temperatures. The 65 kDa protein was phosphorylated only at lower temperatures (between 0 and 15°C). The 30 kDa protein was phosphorylated more at higher temperatures and was possibly a histidine kinase. This protein was present in all the psychrotrophic species studied and in A possible role for these proteins in sensing environmental temperature is proposed.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-140-12-3217
1994-12-01
2021-10-19
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/12/mic-140-12-3217.html?itemId=/content/journal/micro/10.1099/13500872-140-12-3217&mimeType=html&fmt=ahah

References

  1. Bourret R.B., Borkovich K.A., Simon M. Signal transduction pathway involving protein phosphorylation in prokaryotes. Annu Rev Biochem 1991; 60:401–441
    [Google Scholar]
  2. Chauhan S., Shivaji S. Growth and pigmentation in Sphingobacterium antarcticus, a psychrotrophic bacterium from Antarctica. Polar Biol 1994; 14:31–36
    [Google Scholar]
  3. Craig E.A., Gross C.A. Is hsp 70 the cellular thermometer. Trends Biochem Sci 1991; 16:135–140
    [Google Scholar]
  4. Fujitaki J.M., Smith R.A. Techniques in the detection and characterization of phosphoramidate-containing proteins. Methods Enaymol 1984; 107:23–36
    [Google Scholar]
  5. Hoe N.P., Minion F.C., Goguen J.D. Temperature sensing in Yersinia pestis: Regulation olyopF transcription by lcrF. J Bacteriol 1992; 174:4275–4286
    [Google Scholar]
  6. Hoe N.P., Goguen J.D. Temperature sensing in Yersinia pestis: translation of the LcrF activator protein is thermally regulated. J Bacteriol 1993; 175:7901–7909
    [Google Scholar]
  7. Jagannadham M.V., Jayathirtha Rao V., Shivaji S. The major carotenoid pigment of a psychrotrophic Micrococcus roseus: purification, structure and interaction of the pigment with synthetic membranes. J Bacteriol 1991; 173:7911–7917
    [Google Scholar]
  8. Kyhse-Anderson J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods 1984; 10:203–209
    [Google Scholar]
  9. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  10. Maeda K., Imae Y. Thermosensory transduction in Escherichia coli : inhibition of the thermoresponse by L-serine. Proc Natl Acad Sci USA 1979; 76:91–95
    [Google Scholar]
  11. Martensen T.M. Chemical properties, isolation, and analysis of O-phosphates in proteins. Methods in Engymol 1984; 107:3–23
    [Google Scholar]
  12. McCarty J.S., Walker G.C. DnaK as thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc Natl Acad Sci USA 1991; 88:9513–9517
    [Google Scholar]
  13. Mukai K., Kawata M., Tanaka T. Isolation and phosphorylation of the Bacillus subtilis degS and degU gene products. J Biol Chem 1990; 265:20000–20006
    [Google Scholar]
  14. Ray M.K., Shivaji S. Antarctic microorganisms and cold adaptation. In Proceedings of DAE symposium on Molecular Biology of Microorganisms NCL Pune India 1992 Trombay, Bombay: Bhabha Atomic Research Centre; pp 278–283
    [Google Scholar]
  15. Ray M.K., Shivaji S., Shyamala Rao N., Bhargava P.M. Yeast strains from the Schirmacher Oasis, Antarctica. Polar Biol 1989; 9:305–309
    [Google Scholar]
  16. Ray M.K., Seshu Kumar G., Shivaji S. Plasmids from the soil bacteria of Schirmacher Oasis, Antarctica. Microbios 1991; 67:151–157
    [Google Scholar]
  17. Ray M.K., Uma Devi K., Seshu Kumar G., Shivaji S. Extracellular protease from the Antarctic yeast Candida humicola. Appl Environ Microbiol 1992; 58:1918–1923
    [Google Scholar]
  18. Ray M.K., Sitaramamma T., Ghandhi S., Shivaji S. Occurrence and expression of cspA, a cold shock gene in Antarctic psychrotrophic bacteria. FEMS Microbiol Lett 1994a; 116:55–60
    [Google Scholar]
  19. Ray M.K., Seshu Kumar G., Shivaji S. Phosphorylation of lipopolysaccharides in the antarctic psychrotroph Pseudomonas syringae: a possible role in temperature adaptation. J Bacteriol 1994b; 176:4243–4249
    [Google Scholar]
  20. Roy Chowdhury S., Sakai K., Chakrabarty A.M. Alg R2 is an ATP/GTP-dependent protein kinase involved in alginate synthesis by Pseudomonas aeruginosa. Proc Natl Acad Sci USA 1992; 89:2659–2663
    [Google Scholar]
  21. Schnaitman C.A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol 1971; 108:545–552
    [Google Scholar]
  22. Shivaji S., Shyamala Rao N., Saisree L., Sheth V., Reddy G.S.N., Bhargava P.M. Isolation and identification of Micrococcus roseus and Planococcus sp from Schirmacher Oasis, Antarctica. J Biosci 1988; 13:409–414
    [Google Scholar]
  23. Shivaji S., Shyamala Rao N., Saisree L., Sheth V., Reddy G.S.N., Bhargava P.M. Isolation and identification of Pseudomonas sp from Schirmacher Oasis, Antarctica. Appl Environ Microbiol 1989a; 55:767–770
    [Google Scholar]
  24. Shivaji S., Shyamala Rao N., Saisree L., Reddy G.S.N., Seshu Kumar G., Bhargava P.M. Isolates of Arthrobacter from the soils of Schirmacher Oasis, Antarctica. Polar Biol 1989b; 10:225–229
    [Google Scholar]
  25. Shivaji S., Ray M.K., Seshu Kumar G., Reddy G.S.N., Saisree L., Wynn-Williams D.D. Identification of Janthinobacterium lividum from the soils of the islands of Scotia Ridge and from Antarctica peninsula. Polar Biol 1991; 11:267–272
    [Google Scholar]
  26. Shivaji S., Ray M.K., Saisree L., Jagannadham M.V., Seshu Kumar G., Reddy G.S.N., Bhargava P.M. Sphingobacterium antarcticus sp a psychrotrophic halotolerant bacteria from the soils of Schirmacher Oasis, Antarctica. Int J Syst Bacteriol 1992; 42:102–116
    [Google Scholar]
  27. Smith R.A., Halpern R.M., Bruegger B.B., Dunlap A.K., Fricke O. Chromosomal protein phosphorylation on basic amino acids. Methods Cell Biol 1978; 19:153–159
    [Google Scholar]
  28. Stock J.B., Ninfa A.J., Stock A.M. Protein phosphorylation and regulation of adaptive response in bacteria. Microbiol Rev 1989; 53:450–490
    [Google Scholar]
  29. Straus D.B., Walter W.A., Gross C.A. The heat shock response of E. coli is regulated by changes in the concentration of σ32. Nature 1987; 329:348–351
    [Google Scholar]
  30. Straus D.B., Walter W.A., Gross C.A. DnaK, DnaJ and GrpI: heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of σ32. Genes Dev 1990; 4:2202–2209
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-140-12-3217
Loading
/content/journal/micro/10.1099/13500872-140-12-3217
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

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