Rate of reuse of amino acids through proteolysis under hunger conditions

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