---
_id: '14040'
abstract:
- lang: eng
text: Robust oxygenic photosynthesis requires a suite of accessory factors to ensure
efficient assembly and repair of the oxygen-evolving photosystem two (PSII) complex.
The highly conserved Ycf48 assembly factor binds to the newly synthesized D1 reaction
center polypeptide and promotes the initial steps of PSII assembly, but its binding
site is unclear. Here we use cryo-electron microscopy to determine the structure
of a cyanobacterial PSII D1/D2 reaction center assembly complex with Ycf48 attached.
Ycf48, a 7-bladed beta propeller, binds to the amino-acid residues of D1 that
ultimately ligate the water-oxidising Mn4CaO5 cluster, thereby preventing the
premature binding of Mn2+ and Ca2+ ions and protecting the site from damage. Interactions
with D2 help explain how Ycf48 promotes assembly of the D1/D2 complex. Overall,
our work provides valuable insights into the early stages of PSII assembly and
the structural changes that create the binding site for the Mn4CaO5 cluster.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: ScienComp
acknowledgement: P.J.N. and J.W.M. are grateful for the support of the Biotechnology
& Biological Sciences Research Council (awards BB/L003260/1 and BB/P00931X/1). J.
Knoppová, R.S. and J. Komenda were supported by the Czech Science Foundation (project
19-29225X) and by ERC project Photoredesign (no. 854126) and L.A.S. was supported
by the Scientific Service Units (SSU) of IST Austria through resources provided
by the Electron Microscopy Facility (EMF), the Life Science Facility (LSF) and the
IST high-performance computing cluster.
article_number: '4681'
article_processing_charge: Yes
article_type: original
author:
- first_name: Ziyu
full_name: Zhao, Ziyu
last_name: Zhao
- first_name: Irene
full_name: Vercellino, Irene
id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
last_name: Vercellino
orcid: 0000-0001-5618-3449
- first_name: Jana
full_name: Knoppová, Jana
last_name: Knoppová
- first_name: Roman
full_name: Sobotka, Roman
last_name: Sobotka
- first_name: James W.
full_name: Murray, James W.
last_name: Murray
- first_name: Peter J.
full_name: Nixon, Peter J.
last_name: Nixon
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
- first_name: Josef
full_name: Komenda, Josef
last_name: Komenda
citation:
ama: Zhao Z, Vercellino I, Knoppová J, et al. The Ycf48 accessory factor occupies
the site of the oxygen-evolving manganese cluster during photosystem II biogenesis.
Nature Communications. 2023;14. doi:10.1038/s41467-023-40388-6
apa: Zhao, Z., Vercellino, I., Knoppová, J., Sobotka, R., Murray, J. W., Nixon,
P. J., … Komenda, J. (2023). The Ycf48 accessory factor occupies the site of the
oxygen-evolving manganese cluster during photosystem II biogenesis. Nature
Communications. Springer Nature. https://doi.org/10.1038/s41467-023-40388-6
chicago: Zhao, Ziyu, Irene Vercellino, Jana Knoppová, Roman Sobotka, James W. Murray,
Peter J. Nixon, Leonid A Sazanov, and Josef Komenda. “The Ycf48 Accessory Factor
Occupies the Site of the Oxygen-Evolving Manganese Cluster during Photosystem
II Biogenesis.” Nature Communications. Springer Nature, 2023. https://doi.org/10.1038/s41467-023-40388-6.
ieee: Z. Zhao et al., “The Ycf48 accessory factor occupies the site of the
oxygen-evolving manganese cluster during photosystem II biogenesis,” Nature
Communications, vol. 14. Springer Nature, 2023.
ista: Zhao Z, Vercellino I, Knoppová J, Sobotka R, Murray JW, Nixon PJ, Sazanov
LA, Komenda J. 2023. The Ycf48 accessory factor occupies the site of the oxygen-evolving
manganese cluster during photosystem II biogenesis. Nature Communications. 14,
4681.
mla: Zhao, Ziyu, et al. “The Ycf48 Accessory Factor Occupies the Site of the Oxygen-Evolving
Manganese Cluster during Photosystem II Biogenesis.” Nature Communications,
vol. 14, 4681, Springer Nature, 2023, doi:10.1038/s41467-023-40388-6.
short: Z. Zhao, I. Vercellino, J. Knoppová, R. Sobotka, J.W. Murray, P.J. Nixon,
L.A. Sazanov, J. Komenda, Nature Communications 14 (2023).
date_created: 2023-08-13T22:01:13Z
date_published: 2023-08-04T00:00:00Z
date_updated: 2023-12-13T12:06:56Z
day: '04'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1038/s41467-023-40388-6
external_id:
isi:
- '001042606700004'
file:
- access_level: open_access
checksum: 3b9043df3d51c300f9be95eac3ff9d0b
content_type: application/pdf
creator: dernst
date_created: 2023-08-14T07:01:12Z
date_updated: 2023-08-14T07:01:12Z
file_id: '14044'
file_name: 2023_NatureComm_Zhao.pdf
file_size: 2315325
relation: main_file
success: 1
file_date_updated: 2023-08-14T07:01:12Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese
cluster during photosystem II biogenesis
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 14
year: '2023'
...
---
_id: '10182'
abstract:
- lang: eng
text: The mitochondrial oxidative phosphorylation system is central to cellular
metabolism. It comprises five enzymatic complexes and two mobile electron carriers
that work in a mitochondrial respiratory chain. By coupling the oxidation of reducing
equivalents coming into mitochondria to the generation and subsequent dissipation
of a proton gradient across the inner mitochondrial membrane, this electron transport
chain drives the production of ATP, which is then used as a primary energy carrier
in virtually all cellular processes. Minimal perturbations of the respiratory
chain activity are linked to diseases; therefore, it is necessary to understand
how these complexes are assembled and regulated and how they function. In this
Review, we outline the latest assembly models for each individual complex, and
we also highlight the recent discoveries indicating that the formation of larger
assemblies, known as respiratory supercomplexes, originates from the association
of the intermediates of individual complexes. We then discuss how recent cryo-electron
microscopy structures have been key to answering open questions on the function
of the electron transport chain in mitochondrial respiration and how supercomplexes
and other factors, including metabolites, can regulate the activity of the single
complexes. When relevant, we discuss how these mechanisms contribute to physiology
and outline their deregulation in human diseases.
article_processing_charge: No
article_type: original
author:
- first_name: Irene
full_name: Vercellino, Irene
id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
last_name: Vercellino
orcid: ' 0000-0001-5618-3449'
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Vercellino I, Sazanov LA. The assembly, regulation and function of the mitochondrial
respiratory chain. Nature Reviews Molecular Cell Biology. 2022;23:141–161.
doi:10.1038/s41580-021-00415-0
apa: Vercellino, I., & Sazanov, L. A. (2022). The assembly, regulation and function
of the mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology.
Springer Nature. https://doi.org/10.1038/s41580-021-00415-0
chicago: Vercellino, Irene, and Leonid A Sazanov. “The Assembly, Regulation and
Function of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular
Cell Biology. Springer Nature, 2022. https://doi.org/10.1038/s41580-021-00415-0.
ieee: I. Vercellino and L. A. Sazanov, “The assembly, regulation and function of
the mitochondrial respiratory chain,” Nature Reviews Molecular Cell Biology,
vol. 23. Springer Nature, pp. 141–161, 2022.
ista: Vercellino I, Sazanov LA. 2022. The assembly, regulation and function of the
mitochondrial respiratory chain. Nature Reviews Molecular Cell Biology. 23, 141–161.
mla: Vercellino, Irene, and Leonid A. Sazanov. “The Assembly, Regulation and Function
of the Mitochondrial Respiratory Chain.” Nature Reviews Molecular Cell Biology,
vol. 23, Springer Nature, 2022, pp. 141–161, doi:10.1038/s41580-021-00415-0.
short: I. Vercellino, L.A. Sazanov, Nature Reviews Molecular Cell Biology 23 (2022)
141–161.
date_created: 2021-10-24T22:01:35Z
date_published: 2022-02-01T00:00:00Z
date_updated: 2023-08-02T06:55:42Z
day: '01'
department:
- _id: LeSa
doi: 10.1038/s41580-021-00415-0
external_id:
isi:
- '000705697100001'
pmid:
- '34621061'
intvolume: ' 23'
isi: 1
language:
- iso: eng
month: '02'
oa_version: None
page: 141–161
pmid: 1
publication: Nature Reviews Molecular Cell Biology
publication_identifier:
eissn:
- 1471-0080
issn:
- 1471-0072
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: The assembly, regulation and function of the mitochondrial respiratory chain
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 23
year: '2022'
...
---
_id: '12282'
abstract:
- lang: eng
text: From a simple thought to a multicellular movement
acknowledgement: The authors want to thank Professors Carrie Bernecky, Tom Henzinger,
Martin Loose and Gaia Novarino for accepting to be interviewed, thus giving significant
contribution to the discussion that lead to this article.
article_number: '260017'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Nicole
full_name: Amberg, Nicole
id: 4CD6AAC6-F248-11E8-B48F-1D18A9856A87
last_name: Amberg
orcid: 0000-0002-3183-8207
- first_name: Melissa A
full_name: Stouffer, Melissa A
id: 4C9372C4-F248-11E8-B48F-1D18A9856A87
last_name: Stouffer
- first_name: Irene
full_name: Vercellino, Irene
id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
last_name: Vercellino
orcid: 0000-0001-5618-3449
citation:
ama: Amberg N, Stouffer MA, Vercellino I. Operation STEM fatale – how an equity,
diversity and inclusion initiative has brought us to reflect on the current challenges
in cell biology and science as a whole. Journal of Cell Science. 2022;135(8).
doi:10.1242/jcs.260017
apa: Amberg, N., Stouffer, M. A., & Vercellino, I. (2022). Operation STEM fatale
– how an equity, diversity and inclusion initiative has brought us to reflect
on the current challenges in cell biology and science as a whole. Journal of
Cell Science. The Company of Biologists. https://doi.org/10.1242/jcs.260017
chicago: Amberg, Nicole, Melissa A Stouffer, and Irene Vercellino. “Operation STEM
Fatale – How an Equity, Diversity and Inclusion Initiative Has Brought Us to Reflect
on the Current Challenges in Cell Biology and Science as a Whole.” Journal
of Cell Science. The Company of Biologists, 2022. https://doi.org/10.1242/jcs.260017.
ieee: N. Amberg, M. A. Stouffer, and I. Vercellino, “Operation STEM fatale – how
an equity, diversity and inclusion initiative has brought us to reflect on the
current challenges in cell biology and science as a whole,” Journal of Cell
Science, vol. 135, no. 8. The Company of Biologists, 2022.
ista: Amberg N, Stouffer MA, Vercellino I. 2022. Operation STEM fatale – how an
equity, diversity and inclusion initiative has brought us to reflect on the current
challenges in cell biology and science as a whole. Journal of Cell Science. 135(8),
260017.
mla: Amberg, Nicole, et al. “Operation STEM Fatale – How an Equity, Diversity and
Inclusion Initiative Has Brought Us to Reflect on the Current Challenges in Cell
Biology and Science as a Whole.” Journal of Cell Science, vol. 135, no.
8, 260017, The Company of Biologists, 2022, doi:10.1242/jcs.260017.
short: N. Amberg, M.A. Stouffer, I. Vercellino, Journal of Cell Science 135 (2022).
date_created: 2023-01-16T10:03:14Z
date_published: 2022-04-19T00:00:00Z
date_updated: 2023-08-04T10:28:04Z
day: '19'
department:
- _id: SiHi
- _id: LeSa
doi: 10.1242/jcs.260017
external_id:
isi:
- '000798123600015'
pmid:
- '35438168'
intvolume: ' 135'
isi: 1
issue: '8'
language:
- iso: eng
month: '04'
oa_version: None
pmid: 1
publication: Journal of Cell Science
publication_identifier:
eissn:
- 1477-9137
issn:
- 0021-9533
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
scopus_import: '1'
status: public
title: Operation STEM fatale – how an equity, diversity and inclusion initiative has
brought us to reflect on the current challenges in cell biology and science as a
whole
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 135
year: '2022'
...
---
_id: '10146'
abstract:
- lang: eng
text: The enzymes of the mitochondrial electron transport chain are key players
of cell metabolism. Despite being active when isolated, in vivo they associate
into supercomplexes1, whose precise role is debated. Supercomplexes CIII2CIV1-2
(refs. 2,3), CICIII2 (ref. 4) and CICIII2CIV (respirasome)5,6,7,8,9,10 exist in
mammals, but in contrast to CICIII2 and the respirasome, to date the only known
eukaryotic structures of CIII2CIV1-2 come from Saccharomyces cerevisiae11,12 and
plants13, which have different organization. Here we present the first, to our
knowledge, structures of mammalian (mouse and ovine) CIII2CIV and its assembly
intermediates, in different conformations. We describe the assembly of CIII2CIV
from the CIII2 precursor to the final CIII2CIV conformation, driven by the insertion
of the N terminus of the assembly factor SCAF1 (ref. 14) deep into CIII2, while
its C terminus is integrated into CIV. Our structures (which include CICIII2 and
the respirasome) also confirm that SCAF1 is exclusively required for the assembly
of CIII2CIV and has no role in the assembly of the respirasome. We show that CIII2
is asymmetric due to the presence of only one copy of subunit 9, which straddles
both monomers and prevents the attachment of a second copy of SCAF1 to CIII2,
explaining the presence of one copy of CIV in CIII2CIV in mammals. Finally, we
show that CIII2 and CIV gain catalytic advantage when assembled into the supercomplex
and propose a role for CIII2CIV in fine tuning the efficiency of electron transfer
in the electron transport chain.
acknowledged_ssus:
- _id: PreCl
- _id: EM-Fac
- _id: ScienComp
acknowledgement: We thank the pre-clinical facility of the IST Austria and A. Venturino
for assistance with the animals; and V.-V. Hodirnau for assistance during the Titan
Krios data collection, performed at the IST Austria. The data processing was performed
at the IST high-performance computing cluster. This project has received funding
from the European Union’s Horizon 2020 research and innovation program under the
Marie Skłodowska-Curie grant agreement no. 754411.
article_processing_charge: No
article_type: original
author:
- first_name: Irene
full_name: Vercellino, Irene
id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
last_name: Vercellino
orcid: 0000-0001-5618-3449
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Vercellino I, Sazanov LA. Structure and assembly of the mammalian mitochondrial
supercomplex CIII2CIV. Nature. 2021;598(7880):364-367. doi:10.1038/s41586-021-03927-z
apa: Vercellino, I., & Sazanov, L. A. (2021). Structure and assembly of the
mammalian mitochondrial supercomplex CIII2CIV. Nature. Springer
Nature. https://doi.org/10.1038/s41586-021-03927-z
chicago: Vercellino, Irene, and Leonid A Sazanov. “Structure and Assembly of the
Mammalian Mitochondrial Supercomplex CIII2CIV.” Nature. Springer
Nature, 2021. https://doi.org/10.1038/s41586-021-03927-z.
ieee: I. Vercellino and L. A. Sazanov, “Structure and assembly of the mammalian
mitochondrial supercomplex CIII2CIV,” Nature, vol. 598, no.
7880. Springer Nature, pp. 364–367, 2021.
ista: Vercellino I, Sazanov LA. 2021. Structure and assembly of the mammalian mitochondrial
supercomplex CIII2CIV. Nature. 598(7880), 364–367.
mla: Vercellino, Irene, and Leonid A. Sazanov. “Structure and Assembly of the Mammalian
Mitochondrial Supercomplex CIII2CIV.” Nature, vol. 598, no.
7880, Springer Nature, 2021, pp. 364–67, doi:10.1038/s41586-021-03927-z.
short: I. Vercellino, L.A. Sazanov, Nature 598 (2021) 364–367.
date_created: 2021-10-17T22:01:17Z
date_published: 2021-10-14T00:00:00Z
date_updated: 2023-08-14T08:01:21Z
day: '14'
department:
- _id: LeSa
doi: 10.1038/s41586-021-03927-z
ec_funded: 1
external_id:
isi:
- '000704581600001'
pmid:
- '34616041'
intvolume: ' 598'
isi: 1
issue: '7880'
language:
- iso: eng
month: '10'
oa_version: None
page: 364-367
pmid: 1
project:
- _id: 260C2330-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '754411'
name: ISTplus - Postdoctoral Fellowships
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Webpage
relation: press_release
url: https://ist.ac.at/en/news/boosting-the-cells-power-house/
scopus_import: '1'
status: public
title: Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 598
year: '2021'
...
---
_id: '6919'
article_number: eaaw6490
article_processing_charge: No
author:
- first_name: Chao
full_name: Qi, Chao
last_name: Qi
- first_name: Giulio Di
full_name: Minin, Giulio Di
last_name: Minin
- first_name: Irene
full_name: Vercellino, Irene
id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
last_name: Vercellino
orcid: 0000-0001-5618-3449
- first_name: Anton
full_name: Wutz, Anton
last_name: Wutz
- first_name: Volodymyr M.
full_name: Korkhov, Volodymyr M.
last_name: Korkhov
citation:
ama: Qi C, Minin GD, Vercellino I, Wutz A, Korkhov VM. Structural basis of sterol
recognition by human hedgehog receptor PTCH1. Science Advances. 2019;5(9).
doi:10.1126/sciadv.aaw6490
apa: Qi, C., Minin, G. D., Vercellino, I., Wutz, A., & Korkhov, V. M. (2019).
Structural basis of sterol recognition by human hedgehog receptor PTCH1. Science
Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw6490
chicago: Qi, Chao, Giulio Di Minin, Irene Vercellino, Anton Wutz, and Volodymyr
M. Korkhov. “Structural Basis of Sterol Recognition by Human Hedgehog Receptor
PTCH1.” Science Advances. American Association for the Advancement of Science,
2019. https://doi.org/10.1126/sciadv.aaw6490.
ieee: C. Qi, G. D. Minin, I. Vercellino, A. Wutz, and V. M. Korkhov, “Structural
basis of sterol recognition by human hedgehog receptor PTCH1,” Science Advances,
vol. 5, no. 9. American Association for the Advancement of Science, 2019.
ista: Qi C, Minin GD, Vercellino I, Wutz A, Korkhov VM. 2019. Structural basis of
sterol recognition by human hedgehog receptor PTCH1. Science Advances. 5(9), eaaw6490.
mla: Qi, Chao, et al. “Structural Basis of Sterol Recognition by Human Hedgehog
Receptor PTCH1.” Science Advances, vol. 5, no. 9, eaaw6490, American Association
for the Advancement of Science, 2019, doi:10.1126/sciadv.aaw6490.
short: C. Qi, G.D. Minin, I. Vercellino, A. Wutz, V.M. Korkhov, Science Advances
5 (2019).
date_created: 2019-09-29T22:00:45Z
date_published: 2019-09-18T00:00:00Z
date_updated: 2023-08-30T06:55:31Z
day: '18'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1126/sciadv.aaw6490
external_id:
isi:
- '000491128800062'
file:
- access_level: open_access
checksum: b2256c9117655bc15f621ba0babf219f
content_type: application/pdf
creator: kschuh
date_created: 2019-10-02T11:13:54Z
date_updated: 2020-07-14T12:47:44Z
file_id: '6928'
file_name: 2019_AAAS_Qi.pdf
file_size: 1236101
relation: main_file
file_date_updated: 2020-07-14T12:47:44Z
has_accepted_license: '1'
intvolume: ' 5'
isi: 1
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '09'
oa: 1
oa_version: Published Version
publication: Science Advances
publication_identifier:
eissn:
- '23752548'
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural basis of sterol recognition by human hedgehog receptor PTCH1
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2019'
...