Abstract
Wall-less L-forms of Escherichia coli constitute an interesting, and relatively underused, model system for numerous studies of bacterial physiology including the cell cycle, intracellular structure and protein phosphorylation. Total extracts of the L-form revealed a pattern of protein phosphorylation similar to that of an enteropathogenic strain but very different from its parental K-12 strain. In particular, the L-form extract revealed phosphorylation on tyrosine of a protein important in pathogenesis, TypA, and calcium-specific phosphorylation of a 40 kDa protein. Two new phosphoproteins were identified in the L-form as the DNA-binding protein Dps, and YfiD, a protein of 14 kDa with homology to pyruvate formate-lyase and a region containing a tRNA cluster in bacteriophage T5.
| Original language | English |
|---|---|
| Pages (from-to) | 3289-3295 |
| Number of pages | 7 |
| Journal | Microbiology |
| Volume | 144 |
| Issue number | 12 |
| Publication status | Published - 1998 |
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Keywords
- Calcium
- Dps
- TypA
- Tyrosine phosphorylation
- YfiD
ASJC Scopus subject areas
- Microbiology
Cite this
Protein phosphorylation in Escherichia coli L. form NC-7. / Freestone, P.; Grant, S.; Trinei, M.; Onoda, T.; Norris, V.
In: Microbiology, Vol. 144, No. 12, 1998, p. 3289-3295.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Protein phosphorylation in Escherichia coli L. form NC-7
AU - Freestone, P.
AU - Grant, S.
AU - Trinei, M.
AU - Onoda, T.
AU - Norris, V.
PY - 1998
Y1 - 1998
N2 - Wall-less L-forms of Escherichia coli constitute an interesting, and relatively underused, model system for numerous studies of bacterial physiology including the cell cycle, intracellular structure and protein phosphorylation. Total extracts of the L-form revealed a pattern of protein phosphorylation similar to that of an enteropathogenic strain but very different from its parental K-12 strain. In particular, the L-form extract revealed phosphorylation on tyrosine of a protein important in pathogenesis, TypA, and calcium-specific phosphorylation of a 40 kDa protein. Two new phosphoproteins were identified in the L-form as the DNA-binding protein Dps, and YfiD, a protein of 14 kDa with homology to pyruvate formate-lyase and a region containing a tRNA cluster in bacteriophage T5.
AB - Wall-less L-forms of Escherichia coli constitute an interesting, and relatively underused, model system for numerous studies of bacterial physiology including the cell cycle, intracellular structure and protein phosphorylation. Total extracts of the L-form revealed a pattern of protein phosphorylation similar to that of an enteropathogenic strain but very different from its parental K-12 strain. In particular, the L-form extract revealed phosphorylation on tyrosine of a protein important in pathogenesis, TypA, and calcium-specific phosphorylation of a 40 kDa protein. Two new phosphoproteins were identified in the L-form as the DNA-binding protein Dps, and YfiD, a protein of 14 kDa with homology to pyruvate formate-lyase and a region containing a tRNA cluster in bacteriophage T5.
KW - Calcium
KW - Dps
KW - TypA
KW - Tyrosine phosphorylation
KW - YfiD
UR - http://www.scopus.com/inward/record.url?scp=0032442801&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032442801&partnerID=8YFLogxK
M3 - Article
C2 - 9884220
AN - SCOPUS:0032442801
VL - 144
SP - 3289
EP - 3295
JO - Microbiology
JF - Microbiology
SN - 1350-0872
IS - 12
ER -