| Range |
≤30 % of total intracellular protein/hour
|
| Organism |
Unspecified |
| Reference |
Trötschel C, Albaum SP, Poetsch A. Proteome turnover in bacteria: current status for Corynebacterium glutamicum and related bacteria. Microb Biotechnol. 2013 Nov6(6):708-19. doi: 10.1111/1751-7915.12035 p.708 right column 2nd paragraphPubMed ID23425033
|
| Primary Source |
Pine MJ. Turnover of intracellular proteins. Annu Rev Microbiol. 1972 26: 103-26.PubMed ID4562805
|
| Method |
"2D-electrophoresis for turnover determination. One of
the first technologies for tracing newly synthesized
proteins and calculating protein turnover was radioactive
labelling. In the common pulse-chase experiments
(Takahashi and Ono, 2003), the biological material (e.g.
bacteria) is cultivated in the absence of a (radioactive)
tracer, and at a defined time-point the tracer (e.g. a
radioactive amino acid) is added and consumed (pulse
phase) thereupon, the sample is cultivated again without
the tracer and its disappearance, for instance due to
protein degradation, is monitored (chase phase). The
technology has already been applied from microorganisms
to mammals since about 40 years (primary source &
Larrabee et al., 1980)." |
| Comments |
"Even
before the advent of powerful proteome separation techniques
like 2D-electrophoresis and the invention of biological
mass spectrometry, the simple pulse-chase
analysis of total cellular protein delivered a fundamental
insight into bacterial physiology: a generally low protein
degradation rate for growing bacteria experiencing ideal
nutrient supply (Larrabee et al., 1980), and substantial
reuse of amino acids through proteolysis under hunger
conditions (Primary source), which may reach up to 30%/h of
total intracellular protein." |
| Entered by |
Uri M |
| ID |
110437 |