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Literature summary for 5.6.1.5 extracted from

  • Ehlinger, A.; Park, S.; Fahmy, A.; Lary, J.W.; Cole, J.L.; Finley, D.; Walters, K.J.
    Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding (2013), Structure, 21, 753-765.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G360A/G387A site-directed mutagenesis, the Rpt6 mutant reduces the Rpn14 association with proteasome base and disrupts holoenzyme formation in vitro Saccharomyces cerevisiae
additional information Saccharomyces cerevisiae Rpt6-C spans P318-K405 and is a protein with one conformational state displays in the resulting spectrum one backbone amide signal for each amino acid except proline. Generation Rpt6-C protein samples in which lysine, alanine, leucine, or valine were selectively 15N-labeled. Rpt6-C exchanges between a 4-helix bundle and a partially unfolded state that exhibits increased dynamics, Rpt6-C reversibly exchanges between its two conformational states Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q01939 gene RPT6
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Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More three Rpt heterodimeric RP assembly intermediates occur along with four chaperone-like proteins that interact transiently with C-terminal domains of Rpt proteins Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
RP triphosphatase protein
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Saccharomyces cerevisiae
Rpt6
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Saccharomyces cerevisiae
Rpt6 ATPase
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction loss of Rpt6's partially unfolded state by glycine substitution in Rpt6 mutant G360A/G387A disrupts holoenzyme formation in vitro, an effect enhanced by Rpn14. Loss of Rpt6 conformational exchange enhances Rpn14 requirement during proteasome stress. Saccharomyces cerevisiae lacking Rpn14 and with Rpt6 mutant G360A/G387A incorporated demonstrate hallmarks of defective proteasome assembly and synthetic growth defects Saccharomyces cerevisiae
additional information Rpt6's C-terminal domain undergoes dynamic helix-coil transitions enabled by helix-destabilizing glycines within its two most C-terminal alpha-helices. Rpn14 binds selectively to Rpt6's 4-helix bundle, with surprisingly high affinity. The N-terminal ends of alpha2 and alpha4, and the alpha1-alpha2 and alpha3-alpha4 loops are involved in Rpn14-binding Saccharomyces cerevisiae
physiological function juxtaposed to either or both ends of the proteasome core particle a 19S regulatory particle (RP) exists that recognizes and prepares ubiquitinated proteins for proteolysis. RP triphosphatase proteins (Rpt1-Rpt6), which are critical for substrate translocation into the CP, bind chaperone-like proteins (Hsm3, Nas2, Nas6, Rpn14) implicated in RP assembly, effect of Rpn14 and its interaction with Rpt6 during assembly, overview Saccharomyces cerevisiae