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Literature summary for 5.6.1.5 extracted from

  • Lee, S.H.; Moon, J.H.; Yoon, S.K.; Yoon, J.B.
    Stable incorporation of ATPase subunits into 19 S regulatory particle of human proteasome requires nucleotide binding and C-terminal tails (2012), J. Biol. Chem., 287, 9269-9279.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of FLAG-tagged wild-type and mutant subunits Rpt3 and Rpt6 in HeLa cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information disruption of nucleotide binding to an Rpt subunit by mutation in the Walker A motif, mutation in the Walker B motif, deletion of the HbYX motif, C-terminal deletions in Rpts not possessing the HbYX motif Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + polypeptide Homo sapiens
-
ADP + phosphate + unfolded polypeptide
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + polypeptide
-
Homo sapiens ADP + phosphate + unfolded polypeptide
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction disruption of nucleotide binding to an Rpt subunit by mutation in the Walker A motif inhibits the assembly of the Rpt ring without affecting heterodimer formation with its partner Rpt subunit. Coexpression of the base assembly chaperones S5b and PAAF1 with mutant Rpt1 and Rpt6, respectively, relieves assembly inhibition of mutant Rpts by facilitating their interaction with adjacent Rpt dimers. The mutation in the Walker B motif which impairs ATP hydrolysis does not affect Rpt ring formation. Incorporation of a Walker B mutant Rpt subunit abrogates the ATPase activity of the 19S RP, suggesting that failure of the mutant Rpt to undergo the conformational transition from an ATP-bound to an ADP-bound state impairs conformational changes in the other five wild-type Rpts in the Rpt ring. Deletion of the HbYX motif impairs the efficient assembly of the ATPase ring in the 19S RP, whereas C-terminal deletions in Rpts not possessing the HbYX motif do not have any deleterious effect on proteasome assembly Homo sapiens
additional information assembly of the 26S proteasome is a complex process involving formation of ring structures from homologous subunits. Stable incorporation of ATPase subunits into 19S regulatory particle, RP, of human proteasome requires nucleotide binding and C-terminal tails, but not ATP hydrolysis. The C-terminal tails of Rpt subunits possessing core particle (CP)-binding affinities facilitate the cellular assembly of the 19S RP, implying that the 20S core particle may function as a template for base assembly in human cells Homo sapiens