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  In Vivo Dissection of the Intrinsically Disordered Receptor Domain of Tim23

Günsel, U., Paz, E., Gupta, R., Mathes, I., Azem, A., & Mokranjac, D. (2020). In Vivo Dissection of the Intrinsically Disordered Receptor Domain of Tim23. JOURNAL OF MOLECULAR BIOLOGY, 432(10), 3326-3337. doi:10.1016/j.jmb.2020.03.031.

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 Creators:
Günsel, Umut1, Author
Paz, Eyal1, Author
Gupta, Ruhita1, Author
Mathes, Isabella2, Author              
Azem, Abdussalam1, Author
Mokranjac, Dejana1, Author
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1external, ou_persistent22              
2Zachariae, Wolfgang / Chromosome Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565176              

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Free keywords: MITOCHONDRIAL PRESEQUENCE TRANSLOCASE; PROTEIN IMPORT; PREPROTEIN TRANSLOCASE; COMPLEX REVEALS; TIM50; TRANSPORT; INNER; OUTER; TOM; MEMBRANEmitochondria; protein sorting; protein translocation; TIM23 complex; presequence pathway;
 Abstract: In the intermembrane space (IMS) of mitochondria, the receptor domain of Tim23 has an essential role during translocation of hundreds of different proteins from the cytosol via the TOM and TIM23 complexes in the outer and inner membranes, respectively. This intrinsically disordered domain, which can even extend into the cytosol, was shown, mostly in vitro, to interact with several subunits of the TOM and TIM23 complexes. To obtain molecular understanding of this organizational hub in the IMS, we dissected the IMS domain of Tim23 in vivo. We show that the interaction surface of Tim23 with Tim50 is larger than previously thought and reveal an unexpected interaction of Tim23 with Pam17 in the IMS, impairment of which influences their interaction in the matrix. Furthermore, mutations of two conserved negatively charged residues of Tim23, close to the inner membrane, prevented dimerization of Tim23. The same mutations increased exposure of Tim23 on the mitochondrial surface, whereas dissipation of membrane potential decreased it. Our results reveal an intricate network of Tim23 interactions in the IMS, whose influence is transduced across two mitochondrial membranes, ensuring efficient translocation of proteins into mitochondria. (C) 2020 The Author(s). Published by Elsevier Ltd.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000532829100015
DOI: 10.1016/j.jmb.2020.03.031
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Title: JOURNAL OF MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 24-28 OVAL RD, LONDON NW1 7DX, ENGLAND : ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Pages: - Volume / Issue: 432 (10) Sequence Number: - Start / End Page: 3326 - 3337 Identifier: ISSN: 0022-2836