ATP-dependent proteinases in bacteria

Cytoplasmic proteolysis is an indispensable process for proper function of a cell. Degradation of many intracellular proteins is initiated by ATP-dependent proteinases, which are involved in the regulation of the level of proteins with short half-lives. In addition, they remove many damaged and abno...

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Bibliographic Details
Published in:Folia microbiologica 2002-01, Vol.47 (3), p.203-212
Main Authors: HLAVACEK, O, VACHOVA, L
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
ATP
ATP-Dependent Proteases
Bacteria
Bacteria - enzymology
Bacteria - genetics
Bacterial diseases
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Chaperones
Data processing
Domains
Endopeptidases - chemistry
Endopeptidases - genetics
Endopeptidases - metabolism
Ent and stomatologic bacterial diseases
Fundamental and applied biological sciences. Psychology
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
Human bacterial diseases
Infectious diseases
Medical sciences
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Microbiology
Models, Biological
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Polypeptides
Proteinase
Proteins
Proteolysis
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Stress
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Summary:Cytoplasmic proteolysis is an indispensable process for proper function of a cell. Degradation of many intracellular proteins is initiated by ATP-dependent proteinases, which are involved in the regulation of the level of proteins with short half-lives. In addition, they remove many damaged and abnormal proteins and thus play also an important role during stress. ATP-dependent proteinases are large multi-subunit assemblies composed of proteolytic core domains and ATPase-containing regulatory domains on a single polypeptide chain or on distinct subunits, which can act as molecular chaperones. This review briefly summarizes the data about four main groups of these proteinases in bacteria (i.e. Lon, Clp family, HslUV and FtsH) and characterizes their structure, mechanism of action and properties.
ISSN:0015-5632
1874-9356
DOI:10.1007/BF02817639