Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins.
Proteins, like DNA, are subject to various forms of damage that can render them non-functional. Conformational changes and covalent chemical alterations occur spontaneously, and the rates of these reactions can be increased by environmental stresses such as heat, oxidative agents, or changes in pH or osmotic conditions. Although affected proteins can be replaced by de novo biosynthesis, cells--especially those subjected to stress or nutrient limitation--have developed mechanisms which can either restore damaged polypeptides to an active state or remove them. Such mechanisms can spare the biosynthetic capacity of the cell and ensure that the presence of non-functional molecules does not disrupt cell physiology. Three major mechanisms, which operate in bacteria as well as eukaryotic organisms, have been described. First, chaperones not only assist in proper de novo folding of proteins but also provide an important means of restoring activity to conformationally damaged proteins. Second, enzymatic 'repair' systems exist to directly reverse certain forms of protein damage, including proline isomerization, methionine oxidation and the formation of isoaspartyl residues. Finally, proteolysis provides a 'last-resort' means of dealing with abnormal proteins which cannot be repaired. Protein maintenance and repair may be of special importance for bacteria preparing to survive extended periods in stationary phase: both constitutive and induced mechanisms are utilized to permit survival despite greatly reduced protein synthesis.
D000064:Acclimatization; D000591:Amino Acid Isomerases / Q000378:metabolism; D001224:Aspartic Acid; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D004777:Environment; D008961:Models, Structural; D018384:Oxidative Stress; D019696:Peptidylprolyl Isomerase; D011392:Proline / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004220:Disulfides; D001224:Aspartic Acid; D011392:Proline; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase