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Literature summary for 3.4.25.2 extracted from

  • Sundar, S.; McGinness, K.E.; Baker, T.A.; Sauer, R.T.
    Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV (2010), J. Mol. Biol., 403, 420-429.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.25.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged HslU and HslV in Escherichia coli Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information protein binding, e.g. of Escherichia coli ClpS, SspB, or DegS PDZ domain polypeptides, to the C-terminus of substrates selectively slows HslUV degradation, the inhibition affects an early step in degradation. Synergistic effects of N- and C-terminal blocking Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Arc + H2O Escherichia coli N-terminal residues of Arc are important for HslUV degradation ?
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 ?
lambda CI repressor ext1-lambdacIN-RSEYE + H2O Escherichia coli
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 ?
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 ?
additional information Escherichia coli HslU hexamers recognize and unfold native protein substrates and then translocate the polypeptide into the degradation chamber of the HslV peptidase. The degradation appears to consist of discrete steps, which involve the interaction of different terminal sequence signals in the substrate with different receptor sites in the HslUV protease. Mutations in the unstructured N-terminal and C-terminal sequences of two model substrates alter HslUV recognition and degradation kinetics, including changes in Vmax. Blocking either terminus of the substrate interferes with HslUV degradation, with synergistic effects when both termini are obstructed ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged HslU and HslV from Escherichia coli by nickel affinity chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arc + H2O N-terminal residues of Arc are important for HslUV degradation Escherichia coli ?
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 ?
Arc-st11-ssrA + H2O Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 and ssrA tags (Arc-st11-ssrA) Escherichia coli ?
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 ?
Arc-st11-ssrADD + H2O Arc variants with a C-terminal ssrA tag (Arc-ssrA), the st11 tag and a mutant ssrA tag in which the terminal AA sequence is replaced by DD Escherichia coli ?
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 ?
lambda CI repressor ext1-lambdacIN-RSEYE + H2O
-
 Escherichia coli ?
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 ?
lambda cI repressor mutant ext1-lambdacIN-ISVTL + H2O a variant in which the C-terminal sequence is changed from RSEYE to ISVTL, to give ext1-lambdacIN-ISVTL, that HslUV degrades faster than the parental protein, ext1-lambdacIN-RSEYE, by 2fold increase in Vmax Escherichia coli ?
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 ?
additional information HslU hexamers recognize and unfold native protein substrates and then translocate the polypeptide into the degradation chamber of the HslV peptidase. The degradation appears to consist of discrete steps, which involve the interaction of different terminal sequence signals in the substrate with different receptor sites in the HslUV protease. Mutations in the unstructured N-terminal and C-terminal sequences of two model substrates alter HslUV recognition and degradation kinetics, including changes in Vmax. Blocking either terminus of the substrate interferes with HslUV degradation, with synergistic effects when both termini are obstructed Escherichia coli ?
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 ?
additional information modeling of overall reaction by substrate binding and dissociation steps, and by a rate-limiting enzymatic step, which corresponds to substrate engagement, unfolding, or translocation Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
AAA+ protease HslUV
-
 Escherichia coli
HslUV
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli

General Information

General Information Comment Organism
evolution Escherichia coli HslUV protease is a member of a major family of ATP-dependent AAA+ degradation machines Escherichia coli