Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)

Kai Cai; Ronnie O. Frederick; Jin Hae Kim; Nichole M. Reinen; Marco Tonelli; John L. Markley

doi:10.1074/jbc.M113.482042

Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)

Kai Cai
, Ronnie O. Frederick
, Jin Hae Kim
, Nichole M. Reinen
, Marco Tonelli
, John L. Markley

Department of New Biology

University of Wisconsin-Madison

Research output: Contribution to journal › Article › peer-review

53 Scopus citations

Abstract

Background:Iron-sulfur cluster biosynthesis involves a scaffold protein (ISCU), cysteine desulfurase (NFS1), chaperone (mtHSP70), and co-chaperone (HSC20). Results:Human mitochondrial ISCU populates structured (S) and disordered (D) conformational states. S interacts preferentially with NFS1 and mtHSP70; D interacts preferentially with HSC20. Conclusion:Shifts in the S ⇄ D equilibrium reveal functional states. Significance:The scaffold protein metamorphic property seen inEscherichia coliis conserved in humans.

Original language	English
Pages (from-to)	28755-28770
Number of pages	16
Journal	Journal of Biological Chemistry
Volume	288
Issue number	40
DOIs	https://doi.org/10.1074/jbc.M113.482042
State	Published - 4 Oct 2013

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Cai, K., Frederick, R. O., Kim, J. H., Reinen, N. M., Tonelli, M., & Markley, J. L. (2013). Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). Journal of Biological Chemistry, 288(40), 28755-28770. https://doi.org/10.1074/jbc.M113.482042

Cai, Kai ; Frederick, Ronnie O. ; Kim, Jin Hae et al. / Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 40. pp. 28755-28770.

@article{d7c79a8e03fa4b42b15da3b2f810f39e,

title = "Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)",

abstract = "Background:Iron-sulfur cluster biosynthesis involves a scaffold protein (ISCU), cysteine desulfurase (NFS1), chaperone (mtHSP70), and co-chaperone (HSC20). Results:Human mitochondrial ISCU populates structured (S) and disordered (D) conformational states. S interacts preferentially with NFS1 and mtHSP70; D interacts preferentially with HSC20. Conclusion:Shifts in the S ⇄ D equilibrium reveal functional states. Significance:The scaffold protein metamorphic property seen inEscherichia coliis conserved in humans.",

author = "Kai Cai and Frederick, \{Ronnie O.\} and Kim, \{Jin Hae\} and Reinen, \{Nichole M.\} and Marco Tonelli and Markley, \{John L.\}",

year = "2013",

month = oct,

day = "4",

doi = "10.1074/jbc.M113.482042",

language = "English",

volume = "288",

pages = "28755--28770",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "40",

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Cai, K, Frederick, RO, Kim, JH, Reinen, NM, Tonelli, M & Markley, JL 2013, 'Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)', Journal of Biological Chemistry, vol. 288, no. 40, pp. 28755-28770. https://doi.org/10.1074/jbc.M113.482042

Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). / Cai, Kai; Frederick, Ronnie O.; Kim, Jin Hae et al.
In: Journal of Biological Chemistry, Vol. 288, No. 40, 04.10.2013, p. 28755-28770.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)

AU - Cai, Kai

AU - Frederick, Ronnie O.

AU - Kim, Jin Hae

AU - Reinen, Nichole M.

AU - Tonelli, Marco

AU - Markley, John L.

PY - 2013/10/4

Y1 - 2013/10/4

N2 - Background:Iron-sulfur cluster biosynthesis involves a scaffold protein (ISCU), cysteine desulfurase (NFS1), chaperone (mtHSP70), and co-chaperone (HSC20). Results:Human mitochondrial ISCU populates structured (S) and disordered (D) conformational states. S interacts preferentially with NFS1 and mtHSP70; D interacts preferentially with HSC20. Conclusion:Shifts in the S ⇄ D equilibrium reveal functional states. Significance:The scaffold protein metamorphic property seen inEscherichia coliis conserved in humans.

AB - Background:Iron-sulfur cluster biosynthesis involves a scaffold protein (ISCU), cysteine desulfurase (NFS1), chaperone (mtHSP70), and co-chaperone (HSC20). Results:Human mitochondrial ISCU populates structured (S) and disordered (D) conformational states. S interacts preferentially with NFS1 and mtHSP70; D interacts preferentially with HSC20. Conclusion:Shifts in the S ⇄ D equilibrium reveal functional states. Significance:The scaffold protein metamorphic property seen inEscherichia coliis conserved in humans.

UR - https://www.scopus.com/pages/publications/84885117582

U2 - 10.1074/jbc.M113.482042

DO - 10.1074/jbc.M113.482042

M3 - Article

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AN - SCOPUS:84885117582

SN - 0021-9258

VL - 288

SP - 28755

EP - 28770

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 40

ER -

Cai K, Frederick RO, Kim JH, Reinen NM, Tonelli M, Markley JL. Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). Journal of Biological Chemistry. 2013 Oct 4;288(40):28755-28770. doi: 10.1074/jbc.M113.482042

Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)

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