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Molecular extensibility of mini-dystrophins and a dystrophin rod construct.

Abstract：

:Muscular dystrophies arise with various mutations in dystrophin, implicating this protein in force transmission in normal muscle. With 24 three-helix, spectrin repeats interspersed with proline-rich hinges, dystrophin's large size is an impediment to gene therapy, prompting the construction of mini-dystrophins. Results thus far in dystrophic mice suggest that at least one hinge between repeats is necessary though not sufficient for palliative effect. One such mini-dystrophin is studied here in forced extension at the single molecule level. Delta2331 consists of repeats (R) and hinges (H) H1-R1-2 approximately H3 approximately R22-24-H4 linked by native (-) and non-native (approximately) sequence. This is compared to its core fragment R2 approximately H3 approximately R22 as well as an eight-repeat rod fragment middle (RFM: R8-15). We show by atomic force microscopy that all repeats extend and unfold at forces comparable to those that a few myosin molecules can generate. The hinge regions most often extend and transmit force while limiting tandem repeat unfolding. From 23-42 degrees C, the dystrophin constructs also appear less temperature-sensitive in unfolding compared to a well-studied betaI-spectrin construct. The results thus reveal new modes of dystrophin flexibility that may prove central to functions of both dystrophin and mini-dystrophins.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Bhasin N,Law R,Liao G,Safer D,Ellmer J,Discher BM,Sweeney HL,Discher DE

doi

10.1016/j.jmb.2005.07.064

keywords:

subject

Has Abstract

pub_date

2005-09-30 00:00:00

pages

795-806

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)00877-6

journal_volume

352

pub_type

杂志文章

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