The yeast mitochondrial succinylome: Implications for
regulation of mitochondrial nucleoids

J 2021

The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids

FRANKOVSKÝ, Ján, Barbora KERESZTESOVÁ, Jana BELLOVÁ, Nina KUNOVÁ, Nikola ČANIGOVÁ et. al.

Basic information

Original name

The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids

Authors

FRANKOVSKÝ, Ján (703 Slovakia), Barbora KERESZTESOVÁ (703 Slovakia), Jana BELLOVÁ (703 Slovakia), Nina KUNOVÁ (703 Slovakia), Nikola ČANIGOVÁ (703 Slovakia), Kateřina HANÁKOVÁ (203 Czech Republic, belonging to the institution), Jacob A. BAUER (703 Slovakia), Gabriela ONDROVIČOVÁ (703 Slovakia), Veronika LUKÁČOVÁ (703 Slovakia), Barbara SIVÁKOVÁ (703 Slovakia), Zbyněk ZDRÁHAL (203 Czech Republic, guarantor, belonging to the institution), Vladimír PEVALA (703 Slovakia), Katarína PROCHÁZKOVÁ (703 Slovakia), Jozef NOSEK (703 Slovakia), Peter BARÁTH (703 Slovakia), Eva KUTEJOVÁ (703 Slovakia) and Ľubomír TOMÁŠKA (703 Slovakia)

Edition

The Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2021, 0021-9258

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

fulltext

Impact factor

Impact factor: 5.157 in 2020

RIV identification code

RIV/00216224:14740/21:00123803

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.jbc.2021.101155

UT WoS

000713011000011

Keywords in English

DNA–protein interaction lysine succinylation mitochondria mitochondrial DNA mitochondrial nucleoid post-translational modification (PTM) proteomics succinylome yeast

Abstract

V originále

Acylation modifications, such as the succinylation of lysine, are post-translational modifications and a powerful means of regulating protein activity. Some acylations occur non enzymatically, driven by an increase in the concentration of acyl group donors. Lysine succinylation has a profound effect on the corresponding site within the protein, as it dramatically changes the charge of the residue. In eukaryotes, it predominantly affects mitochondrial proteins because the donor of succinate, succinyl-CoA, is primarily generated in the tricarboxylic acid cycle. Although numerous succinylated mitochondrial proteins have been identified in Saccharomyces cerevisiae, a more detailed characterization of the yeast mitochondrial succinylome is still lacking. Here, we performed a proteomic MS analysis of purified yeast mitochondria and detected 314 succinylated mitochondrial proteins with 1763 novel succinylation sites. The mitochondrial nucleoid, a complex of mitochondrial DNA and mitochondrial proteins, is one of the structures whose protein components are affected by succinylation. We found that Abf2p, the principal component of mitochondrial nucleoids responsible for compacting mitochondrial DNA in S. cerevisiae, can be succinylated in vivo on at least thirteen lysine residues. Abf2p succinylation in vitro inhibits its DNA-binding activity and reduces its sensitivity to digestion by the ATP-dependent ScLon protease. We conclude that changes in the metabolic state of a cell resulting in an increase in the concentration of tricarboxylic acid intermediates may affect mitochondrial functions.

Links

90127, large research infrastructures

Name: CIISB II

Citovat

FRANKOVSKÝ, Ján, Barbora KERESZTESOVÁ, Jana BELLOVÁ, Nina KUNOVÁ, Nikola ČANIGOVÁ, Kateřina HANÁKOVÁ, Jacob A. BAUER, Gabriela ONDROVIČOVÁ, Veronika LUKÁČOVÁ, Barbara SIVÁKOVÁ, Zbyněk ZDRÁHAL, Vladimír PEVALA, Katarína PROCHÁZKOVÁ, Jozef NOSEK, Peter BARÁTH, Eva KUTEJOVÁ and Ľubomír TOMÁŠKA. The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. The Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology, 2021, vol. 297, No 4, p. "101155", 16 pp. ISSN 0021-9258. Available from: https://dx.doi.org/10.1016/j.jbc.2021.101155.

@article{1823286,
   author = {Frankovský, Ján and Keresztesová, Barbora and Bellová, Jana and Kunová, Nina and Čanigová, Nikola and Hanáková, Kateřina and Bauer, Jacob A. and Ondrovičová, Gabriela and Lukáčová, Veronika and Siváková, Barbara and Zdráhal, Zbyněk and Pevala, Vladimír and Procházková, Katarína and Nosek, Jozef and Baráth, Peter and Kutejová, Eva and Tomáška, Ľubomír},
   article_number = {4},
   doi = {http://dx.doi.org/10.1016/j.jbc.2021.101155},
   keywords = {DNA–protein interaction lysine succinylation mitochondria mitochondrial DNA mitochondrial nucleoid post-translational modification (PTM) proteomics succinylome yeast},
   language = {eng},
   issn = {0021-9258},
   journal = {The Journal of Biological Chemistry},
   title = {The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids},
   url = {https://www.sciencedirect.com/science/article/pii/S0021925821009571?via%3Dihub},
   volume = {297},
   year = {2021}
}

TY  - JOUR
ID  - 1823286
AU  - Frankovský, Ján - Keresztesová, Barbora - Bellová, Jana - Kunová, Nina - Čanigová, Nikola - Hanáková, Kateřina - Bauer, Jacob A. - Ondrovičová, Gabriela - Lukáčová, Veronika - Siváková, Barbara - Zdráhal, Zbyněk - Pevala, Vladimír - Procházková, Katarína - Nosek, Jozef - Baráth, Peter - Kutejová, Eva - Tomáška, Ľubomír
PY  - 2021
TI  - The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids
JF  - The Journal of Biological Chemistry
VL  - 297
IS  - 4
SP  - "101155"
EP  - "101155"
PB  - American Society for Biochemistry and Molecular Biology
SN  - 00219258
KW  - DNA–protein interaction lysine succinylation mitochondria mitochondrial DNA mitochondrial nucleoid post-translational modification (PTM) proteomics succinylome yeast
UR  - https://www.sciencedirect.com/science/article/pii/S0021925821009571?via%3Dihub
N2  - Acylation modifications, such as the succinylation of lysine, are post-translational modifications and a powerful means of regulating protein activity. Some acylations occur non enzymatically, driven by an increase in the concentration of acyl group donors. Lysine succinylation has a profound effect on the corresponding site within the protein, as it dramatically changes the charge of the residue. In eukaryotes, it predominantly affects mitochondrial proteins because the donor of succinate, succinyl-CoA, is primarily generated in the tricarboxylic acid cycle. Although numerous succinylated mitochondrial proteins have been identified in Saccharomyces cerevisiae, a more detailed characterization of the yeast mitochondrial succinylome is still lacking. Here, we performed a proteomic MS analysis of purified yeast mitochondria and detected 314 succinylated mitochondrial proteins with 1763 novel succinylation sites. The mitochondrial nucleoid, a complex of mitochondrial DNA and mitochondrial proteins, is one of the structures whose protein components are affected by succinylation. We found that Abf2p, the principal component of mitochondrial nucleoids responsible for compacting mitochondrial DNA in S. cerevisiae, can be succinylated in vivo on at least thirteen lysine residues. Abf2p succinylation in vitro inhibits its DNA-binding activity and reduces its sensitivity to digestion by the ATP-dependent ScLon protease. We conclude that changes in the metabolic state of a cell resulting in an increase in the concentration of tricarboxylic acid intermediates may affect mitochondrial functions.
ER  -

FRANKOVSKÝ, Ján, Barbora KERESZTESOVÁ, Jana BELLOVÁ, Nina KUNOVÁ, Nikola ČANIGOVÁ, Kateřina HANÁKOVÁ, Jacob A. BAUER, Gabriela ONDROVIČOVÁ, Veronika LUKÁČOVÁ, Barbara SIVÁKOVÁ, Zbyněk ZDRÁHAL, Vladimír PEVALA, Katarína PROCHÁZKOVÁ, Jozef NOSEK, Peter BARÁTH, Eva KUTEJOVÁ and Ľubomír TOMÁŠKA. The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. \textit{The Journal of Biological Chemistry}. American Society for Biochemistry and Molecular Biology, 2021, vol.~297, No~4, p.~''101155'', 16 pp. ISSN~0021-9258. Available from: https://dx.doi.org/10.1016/j.jbc.2021.101155.

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