NDLI: Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states

Content Provider	PubMed Central
Author	Saitoh, Takashi Mayumi, Igura Obita, Takayuki Ose, Toyoyuki Kojima, Rieko Maenaka, Katsumi Endo, Toshiya Kohda, Daisuke
Copyright Year	2007
Abstract	Most mitochondrial proteins are synthesized in the cytosol and imported into mitochondria. The N-terminal presequences of mitochondrial-precursor proteins contain a diverse consensus motif (φχχφφ, φ is hydrophobic and χ is any amino acid), which is recognized by the Tom20 protein on the mitochondrial surface. To reveal the structural basis of the broad selectivity of Tom20, the Tom20–presequence complex was crystallized. Tethering a presequence peptide to Tom20 through a disulfide bond was essential for crystallization. Unexpectedly, the two crystals with different linker designs provided unique relative orientations of the presequence with respect to Tom20, and neither configuration could fully account for the hydrophobic preference at the three hydrophobic positions of the consensus motif. We propose the existence of a dynamic equilibrium in solution among multiple states including the two bound states. In accordance, NMR 15N relaxation analyses suggested motion on a sub-millisecond timescale at the Tom20–presequence interface. We suggest that the dynamic, multiple-mode interaction is the molecular mechanism facilitating the broadly selective specificity of the Tom20 receptor toward diverse mitochondrial presequences.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7601888
Ending Page	4787
Page Count	11
Starting Page	4777
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	22
Volume Number	26
Language	English
Publisher	Nature Publishing Group
Publisher Date	2007-11-14
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

A hyper-dynamic equilibrium between promoter-bound and nucleoplasmic dimers controls NF-κB-dependent gene activity

NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain

A fast dynamic mode of the EF-G-bound ribosome

Regulation of mitochondrial morphology through proteolytic cleavage of OPA1

Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins

Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.

Regulation of checkpoint kinases through dynamic interaction with Crb2

Different import pathways through the mitochondrial intermembrane space for inner membrane proteins.

YscU recognizes translocators as export substrates of the Yersinia injectisome

Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states

Similar Documents

A hyper-dynamic equilibrium between promoter-bound and nucleoplasmic dimers controls NF-κB-dependent gene activity

NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain

A fast dynamic mode of the EF-G-bound ribosome

Regulation of mitochondrial morphology through proteolytic cleavage of OPA1

Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins

Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.

Regulation of checkpoint kinases through dynamic interaction with Crb2

Different import pathways through the mitochondrial intermembrane space for inner membrane proteins.

YscU recognizes translocators as export substrates of the Yersinia injectisome

Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states