Protein phosphorylation in response to stress in Clostridium acetobutylicum

Journal Article · Sun Jul 01 04:00:00 EDT 1990 · Applied and Environmental Microbiology; (USA)

OSTI ID:5852775

Balodimos, I A; Rapaport, E; Kashket, E R ^[1]

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1. Boston Univ. School of Medicine, MA (USA)

The possible involvement of protein phosphorylation in the clostridial stress response was investigated by radioactively labeling growing cells of Clostridium acetobutylicum with {sup 32}P{sub i} or cell extracts with ({gamma}-{sup 32}P)ATP. Several phosphoproteins were identified; these were not affected by the growth stage of the culture. Although the extent of protein phosphorylation was increased by heat stress, the phosphoproteins did not correspond to known stress proteins seen in one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified clostridial DnaK, a stress protein, acted as a kinase catalyzing the phosphorylation of a 50-kilodalton protein. The phosphorylation of this protein was enhanced in extracts prepared from heat-stressed cells. Diadenosine-5{prime},5{double prime}{prime}-P{sup 1},P{sup 4}-tetraphosphate had no influence on protein phosphorylation.

• OSTI ID: 5852775
• Journal Information: Applied and Environmental Microbiology; (USA), Journal Name: Applied and Environmental Microbiology; (USA) Vol. 56:7; ISSN 0099-2240; ISSN AEMID
• Country of Publication: United States
• Language: English

Related Subjects

551001* -- Physiological Systems-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ATP
BACTERIA
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL EFFECTS
BIOLOGICAL STRESS
CHEMICAL REACTIONS
CLOSTRIDIUM
CLOSTRIDIUM ACETOBUTYLICUM
DAYS LIVING RADIOISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
METHANOGENIC BACTERIA
MICROORGANISMS
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PHOSPHORUS 32
PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORYLATION
PHYSIOLOGY
PROTEINS
RADIOISOTOPES
TRACER TECHNIQUES