Inactivation of the 20S proteasome maturase, Ump1p, leads to the instability of mtDNA in Saccharomyces cerevisiae

Malc, Ewa; Dzierzbicki, Piotr; Kaniak, Aneta; Skoneczna, Adrianna; Ciesla, Zygmunt

doi:10.1016/j.mrfmmm.2009.05.008

Cited by 23 publications

(17 citation statements)

References 46 publications

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“…For example, loss of the 20S assembly chaperone Ump1 causes elevated levels of petite formation (Malc et al, 2009). This has been attributed to mitochondrial DNA damage due to increased production of reactive oxygen species (ROS) coupled with diminished levels of DNA repair (Malc et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

Structure of a Blm10 Complex Reveals Common Mechanisms for Proteasome Binding and Gate Opening

et al. 2010

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Summary The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here we report a 3.4Å resolution crystal structure of a proteasome-Blm10 complex, which reveals that Blm10 surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely closed dome that is expected to restrict access of potential substrates. This architecture, and the observation that Blm10 induces a disordered proteasome gate structure, challenges the assumption that Blm10 functions as an activator of proteolysis in vivo. The Blm10 C-terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators, and indicates a unified model for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial function. Consistent with the structural data, the C-terminal residues of Blm10 are needed for this activity.

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Section: Resultsmentioning

confidence: 99%

Structure of a Blm10 Complex Reveals Common Mechanisms for Proteasome Binding and Gate Opening

et al. 2010

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“…Previous studies have shown a role for the 19S regulatory complex (27) and the proteasome assembly chaperone Ump1 (28) in mitochondrial function, and we have previously shown that the proteasome binding partner Blm10 functions in a mitochon- Table S2) were tested as described under "Experimental Procedures." pba1-⌬, pba2-⌬, and rpn4-⌬ indicate complete deletion of the ORFs.…”

Section: The C Termini Of Pba1-pba2 Contribute To Their Physiologicalmentioning

confidence: 99%

Structure of a Proteasome Pba1-Pba2 Complex

Stadtmueller

Kish-Trier

Ferrell

et al. 2012

Journal of Biological Chemistry

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Background: Pba1-Pba2 facilitates proteasome ␣-ring assembly. Results: Pba1-Pba2 binds mature proteasomes using C-terminal motifs and sequesters ␣-subunit N termini. It does not activate and is not degraded by isolated 20S proteasomes. Conclusion: Pba1-Pba2 is important for proteasome-dependent maintenance of mitochondrial function. The structure is consistent with multiple roles in proteasome assembly. Significance: Models of proteasome assembly and Pba1-Pba2 proteasome function are advanced.

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“…ROS accumulation due to mitochondrial disorder causes destabilization of the mitochondrial and/or nuclear genome. (35,36) BE and its polyphenols effectively suppressed AAPH-induced ROS accumulation in not only cytoplasm but also nuclear (Fig. 4).…”

Section: Discussionmentioning

confidence: 85%

Black soybean seed coat polyphenols prevent AAPH-induced oxidative DNA-damage in HepG2 cells

Yoshioka

Zhang

et al. 2017

J. Clin. Biochem. Nutr.

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Black soybean seed coat extract (BE), which contains abundant polyphenols such as procyanidins, cyanidin 3-glucoside, (+)-catechin, and (−)epicatechin, has been reported on health beneficial functions such as antioxidant activity, anti-inflammatory, anti-obesity, and anti-diabetic activities. In this study, we investigated that prevention of BE and its polyphenols on 2,2'-azobis(2-methylpropionamide) dihydrochloride (AAPH)-induced oxidative DNA damage, and found that these polyphenols inhibited AAPH-induced formation of 8-hydroxy-2'-deoxyguanosine (8-OHdG) as a biomarker for oxidative DNA damage in HepG2 cells. Under the same conditions, these polyphenols also inhibited AAPH-induced accumulation of reactive oxygen species (ROS) in the cells. Inhibition of ROS accumulation was observed in both cytosol and nucleus. It was confirmed that these polyphenols inhibited formation of AAPH radical using oxygen radical absorbance capacity assay under the cell-free conditions. These results indicate that polyphenols in BE inhibit free radical-induced oxidative DNA damages by their potent antioxidant activity. Thus, BE is an effective food material for prevention of oxidative stress and oxidative DNA damages.

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Inactivation of the 20S proteasome maturase, Ump1p, leads to the instability of mtDNA in Saccharomyces cerevisiae

Cited by 23 publications

References 46 publications

Structure of a Blm10 Complex Reveals Common Mechanisms for Proteasome Binding and Gate Opening

Structure of a Blm10 Complex Reveals Common Mechanisms for Proteasome Binding and Gate Opening

Structure of a Proteasome Pba1-Pba2 Complex

Black soybean seed coat polyphenols prevent AAPH-induced oxidative DNA-damage in HepG2 cells

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