The essential cysteines in the CIPC motif of the
thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do
not form an intramolecular disulfide bridge in vivo

J 2022

The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo

KAUROV, Iosif, Jiří HELLER, Sebastian DEISENHAMMER, David POTĚŠIL, Zbyněk ZDRÁHAL et. al.

Základní údaje

Originální název

The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo

Autoři

KAUROV, Iosif (203 Česká republika), Jiří HELLER (203 Česká republika), Sebastian DEISENHAMMER (203 Česká republika), David POTĚŠIL (203 Česká republika, domácí), Zbyněk ZDRÁHAL (203 Česká republika, garant, domácí) a Hassan HASHIMI (203 Česká republika)

Vydání

MOLECULAR AND BIOCHEMICAL PARASITOLOGY, NETHERLANDS, ELSEVIER, 2022, 0166-6851

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

fulltext

Impakt faktor

Impact factor: 1.500

Kód RIV

RIV/00216224:14740/22:00125952

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.molbiopara.2022.111463

UT WoS

000787886300003

Klíčová slova anglicky

Trypanosoma Mitochondrion MICOS Protein import Intermembrane space Oxidative folding

Štítky

CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 10. 10. 2024 15:05, Ing. Martina Blahová

Anotace

V originále

The mitochondrial protein import machinery of trypanosomatids is highly divergent from that of the well-studied models such as baker's yeast. A notable example is that the central catalyst of the mitochondrial intermembrane space import and assembly pathway (MIA), named Mia40, is missing in trypanosomatids. Mia40 works in a two-step process. First it recognizes by direct binding reduced MIA substrate proteins and then catalyzes their oxidative folding to produce intramolecular disulfide bridges. It was recently proposed that a thioredoxin-like subunit of the trypanosomal mitochondrial contact site and cristae organizing system (MICOS) called TbMic20 may be the Mia40 replacement. Our study performed on procyclic stage of the parasite revealed that each of the two cysteines in TbMic20's active site is essential for the stability of MIA substrate proteins although they do not form a disulfide bridge in vivo. The two cysteines of Mia40 & PRIME;s active site form an intramolecular di-sulfide bridge at steady state, which is a prerequisite for its oxidative folding of MIA substrates. Thus, we conclude that TbMic20 is unlikely to represent a bona fide Mia40 replacement and plays a still unresolved role in the stability and/or import of MIA substrates in trypanosomatids. Despite this, the effect of TbMic20 depletion and mutation indicates that the trypanosomal MICOS complex still plays a vital role in the maturation and/or stability of proteins imported by the MIA pathway.

Návaznosti

LM2018127, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

KAUROV, Iosif, Jiří HELLER, Sebastian DEISENHAMMER, David POTĚŠIL, Zbyněk ZDRÁHAL a Hassan HASHIMI. The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo. MOLECULAR AND BIOCHEMICAL PARASITOLOGY. NETHERLANDS: ELSEVIER, 2022, roč. 248, MAR, s. "111463", 10 s. ISSN 0166-6851. Dostupné z: https://dx.doi.org/10.1016/j.molbiopara.2022.111463.

@article{1858757,
   author = {Kaurov, Iosif and Heller, Jiří and Deisenhammer, Sebastian and Potěšil, David and Zdráhal, Zbyněk and Hashimi, Hassan},
   article_location = {NETHERLANDS},
   article_number = {MAR},
   doi = {http://dx.doi.org/10.1016/j.molbiopara.2022.111463},
   keywords = {Trypanosoma Mitochondrion MICOS Protein import Intermembrane space Oxidative folding},
   language = {eng},
   issn = {0166-6851},
   journal = {MOLECULAR AND BIOCHEMICAL PARASITOLOGY},
   title = {The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo},
   url = {http://www.sciencedirect.com/science/article/pii/S0166685122000172},
   volume = {248},
   year = {2022}
}

TY  - JOUR
ID  - 1858757
AU  - Kaurov, Iosif - Heller, Jiří - Deisenhammer, Sebastian - Potěšil, David - Zdráhal, Zbyněk - Hashimi, Hassan
PY  - 2022
TI  - The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo
JF  - MOLECULAR AND BIOCHEMICAL PARASITOLOGY
VL  - 248
IS  - MAR
SP  - "111463"
EP  - "111463"
PB  - ELSEVIER
SN  - 01666851
KW  - Trypanosoma Mitochondrion MICOS Protein import Intermembrane space Oxidative folding
UR  - http://www.sciencedirect.com/science/article/pii/S0166685122000172
N2  - The mitochondrial protein import machinery of trypanosomatids is highly divergent from that of the well-studied models such as baker's yeast. A notable example is that the central catalyst of the mitochondrial intermembrane space import and assembly pathway (MIA), named Mia40, is missing in trypanosomatids. Mia40 works in a two-step process. First it recognizes by direct binding reduced MIA substrate proteins and then catalyzes their oxidative folding to produce intramolecular disulfide bridges. It was recently proposed that a thioredoxin-like subunit of the trypanosomal mitochondrial contact site and cristae organizing system (MICOS) called TbMic20 may be the Mia40 replacement. Our study performed on procyclic stage of the parasite revealed that each of the two cysteines in TbMic20's active site is essential for the stability of MIA substrate proteins although they do not form a disulfide bridge in vivo. The two cysteines of Mia40 & PRIME;s active site form an intramolecular di-sulfide bridge at steady state, which is a prerequisite for its oxidative folding of MIA substrates. Thus, we conclude that TbMic20 is unlikely to represent a bona fide Mia40 replacement and plays a still unresolved role in the stability and/or import of MIA substrates in trypanosomatids. Despite this, the effect of TbMic20 depletion and mutation indicates that the trypanosomal MICOS complex still plays a vital role in the maturation and/or stability of proteins imported by the MIA pathway.
ER  -

KAUROV, Iosif, Jiří HELLER, Sebastian DEISENHAMMER, David POTĚŠIL, Zbyněk ZDRÁHAL a Hassan HASHIMI. The essential cysteines in the CIPC motif of the thioredoxin-like Trypanosoma brucei MICOS subunit TbMic20 do not form an intramolecular disulfide bridge in vivo. \textit{MOLECULAR AND BIOCHEMICAL PARASITOLOGY}. NETHERLANDS: ELSEVIER, 2022, roč.~248, MAR, s.~''111463'', 10 s. ISSN~0166-6851. Dostupné z: https://dx.doi.org/10.1016/j.molbiopara.2022.111463.

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