PXD007155

PXD007155 is an original dataset announced via ProteomeXchange.

Title	INA complex liaises the F1Fo-ATP synthase membrane motor modules - Ina22-Flag pulldown experiments
Description	The F1Fo-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor section forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To prevent unrestricted proton flow dissipating the H+-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA complex (INAC) acts at this decisive step promoting Atp9 ring association with Atp6. INAC binds initially to newly synthesized mitochondrial-encoded Atp6 and Atp8 in complex with maturation factors. INAC association is retained until the F1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1Fo-ATP synthase in a primed state for the terminal assembly step – channel and motor module formation.
HostingRepository	PRIDE
AnnounceDate	2017-11-03
AnnouncementXML	Submission_2017-11-03_08:29:42.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2017-07-31 01:57:34	ID requested
⏵ 1	2017-11-03 08:29:43	announced

Naumenko N, Morgenstern M, Ruckt, ä, schel R, Warscheid B, Rehling P, -ATP synthase membrane motor modules. Nat Commun, 8(1):1237(2017) [pubmed]

curator keyword: Biological

submitter keyword: Saccharomyces cerevisiae, interaction proteomics

Prof. Dr. Bettina Warscheid
contact affiliation	Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg im Breisgau, Germany
contact email	Bettina.Warscheid@biologie.uni-freiburg.de
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/11/PXD007155

PRIDE project URI

• PRIDE
  1. PXD007155
     1. Label: PRIDE project
     2. Name: INA complex liaises the F1Fo-ATP synthase membrane motor modules - Ina22-Flag pulldown experiments