Divalent cations induce a compaction of intrinsically disordered myelin basic protein

被引：47

作者：

Baran, Christian ^{[1
]}

Smith, Graham S. T. ^{[2
]}

Bamm, Vladimir V. ^{[2
]}

Harauz, George ^{[2
]}

Lee, Jeremy S. ^{[1
]}

机构：

[1] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada

[2] Univ Guelph, Dept Mol & Cellular Biol, Guelph, ON N1G 2W1, Canada

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 391卷 / 01期

基金：

加拿大自然科学与工程研究理事会; 加拿大健康研究院;

关键词：

Myelin basic protein (MBP); Multiple sclerosis; Intrinsically disordered protein; Induced folding; Nanopore analysis; 3-DIMENSIONAL STRUCTURE; NANOPORE ANALYSIS; ZINC; TRANSPORT; PEPTIDES; BINDING; FORM; TAU;

D O I：

10.1016/j.bbrc.2009.11.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Central nervous system myelin is a dynamic entity arising from membrane processes extended from oligodendrocytes, which form a tightly-wrapped multilamellar structure around neurons In mature myelin, the predominant splice isoform of classic MBP is 18.5 kDa In solution. MBP is an extended, intrinsically disordered protein with a large effective protein surface for myriad interactions. and possesses transient. and/or induced ordered secondary Structure elements for molecular association or recognition Here, we show by nanopore analysis that the divalent cations copper and zinc induce a compaction of the extended protein In vitro, suggestive of a tertiary conformation that may reflect its arrangement in myelin. (c) 2009 Elsevier Inc All rights reserved

引用

页码：224 / 229

页数：6

共 27 条

[1] An Arg/Lys→Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis [J].

Bates, IR ;

Libich, DS ;

Wood, DD ;

Moscarello, MA ;

Harauz, G .

PROTEIN EXPRESSION AND PURIFICATION, 2002, 25 (02) :330-341

[2] Characterization of a recombinant murine 18.5-kDa myelin basic protein [J].

Bates, IR ;

Matharu, P ;

Ishiyama, N ;

Rochon, D ;

Wood, DD ;

Polverini, E ;

Moscarello, MA ;

Viner, NJ ;

Harauz, G .

PROTEIN EXPRESSION AND PURIFICATION, 2000, 20 (02) :285-299

[3] Three-dimensional structure of myelin basic protein .1. Reconstruction via angular reconstitution of randomly oriented single particles [J].

Beniac, DR ;

Luckevich, MD ;

Czarnota, GJ ;

Tompkins, TA ;

Ridsdale, RA ;

Ottensmeyer, FP ;

Moscarello, MA ;

Harauz, G .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (07) :4261-4268

[4] DIVALENT METALS OF MYELIN AND THEIR DIFFERENTIAL BINDING BY MYELIN BASIC-PROTEIN OF BOVINE CENTRAL-NERVOUS-SYSTEM [J].

BERLET, HH ;

BISCHOFF, H ;

WEINHARDT, F .

NEUROSCIENCE LETTERS, 1994, 179 (1-2) :75-78

[5] Myelin basic protein: a multifunctional protein [J].

Boggs, J. M. .

CELLULAR AND MOLECULAR LIFE SCIENCES, 2006, 63 (17) :1945-1961

[6]

Boggs J.M., 2008, Myelin basic protein

[7] MYELIN BASIC-PROTEIN INTERACTION WITH ZINC AND PHOSPHATE - FLUORESCENCE STUDIES ON THE WATER-SOLUBLE FORM OF THE PROTEIN [J].

CAVATORTA, P ;

GIOVANELLI, S ;

BOBBA, A ;

RICCIO, P ;

SZABO, AG ;

QUAGLIARIELLO, E .

BIOPHYSICAL JOURNAL, 1994, 66 (04) :1174-1179

[8] ZINC IONS STABILIZE THE ASSOCIATION OF BASIC-PROTEIN WITH BRAIN MYELIN MEMBRANES [J].

EARL, C ;

CHANTRY, A ;

MOHAMMAD, N ;

GLYNN, P .

JOURNAL OF NEUROCHEMISTRY, 1988, 51 (03) :718-724

[9] Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations [J].

Goodrich, Carl P. ;

Kirmizialtin, Serdal ;

Huyghues-Despointes, Beatrice M. ;

Zhu, Aiping ;

Scholtz, J. Martin ;

Makarov, Dmitrii E. ;

Movileanu, Liviu .

JOURNAL OF PHYSICAL CHEMISTRY B, 2007, 111 (13) :3332-3335

[10] Myelin basic protein -: diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis [J].

Harauz, G ;

Ishiyama, N ;

Hill, CMD ;

Bates, IR ;

Libich, DS ;

Farés, C .

MICRON, 2004, 35 (07) :503-542

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