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Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners

P. Sharma, E. Maklashina, M. Voehler, S. Balintova, S. Dvorakova, M. Kraus, K. Hadrava Vanova, Z. Nahacka, R. Zobalova, S. Boukalova, K. Cunatova, T. Mracek, HK. Ghayee, K. Pacak, J. Rohlena, J. Neuzil, G. Cecchini, TM. Iverson

. 2024 ; 15 (1) : 473. [pub] 20240111

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc24007596

Grantová podpora
IK6 BX004215 BLRD VA - United States
R01 GM061606 NIGMS NIH HHS - United States
R35 GM118089 NIGMS NIH HHS - United States
S10 RR025677 NCRR NIH HHS - United States

Complex II (CII) activity controls phenomena that require crosstalk between metabolism and signaling, including neurodegeneration, cancer metabolism, immune activation, and ischemia-reperfusion injury. CII activity can be regulated at the level of assembly, a process that leverages metastable assembly intermediates. The nature of these intermediates and how CII subunits transfer between metastable complexes remains unclear. In this work, we identify metastable species containing the SDHA subunit and its assembly factors, and we assign a preferred temporal sequence of appearance of these species during CII assembly. Structures of two species show that the assembly factors undergo disordered-to-ordered transitions without the appearance of significant secondary structure. The findings identify that intrinsically disordered regions are critical in regulating CII assembly, an observation that has implications for the control of assembly in other biomolecular complexes.

Citace poskytuje Crossref.org

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$a Complex II (CII) activity controls phenomena that require crosstalk between metabolism and signaling, including neurodegeneration, cancer metabolism, immune activation, and ischemia-reperfusion injury. CII activity can be regulated at the level of assembly, a process that leverages metastable assembly intermediates. The nature of these intermediates and how CII subunits transfer between metastable complexes remains unclear. In this work, we identify metastable species containing the SDHA subunit and its assembly factors, and we assign a preferred temporal sequence of appearance of these species during CII assembly. Structures of two species show that the assembly factors undergo disordered-to-ordered transitions without the appearance of significant secondary structure. The findings identify that intrinsically disordered regions are critical in regulating CII assembly, an observation that has implications for the control of assembly in other biomolecular complexes.
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