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Assembly properties of two CNBr fragments of avian desmin that correspond to the headpiece domain and helix 1B.

Abstract：

:To study how different domains of the muscle-specific intermediate filament protein, desmin, contribute to its polymerization, two of its CNBr fragments were examined as to their oligomeric structure under assembly conditions. One of these, D88, covers residues 1-88 and represents almost the entire headpiece; the other, D109, covers residues 145-254, and includes the entire Helix 1B and part of linker L12 of the intact molecule. Chemical cross-linking followed by SDS-PAGE, and analytical gel filtration, revealed that in 10 mM Tris-HCl, pH 8.5, conditions that favor tetramerization of intact desmin D88 formed only dimers. D109, on the other hand, formed primarily a dimeric species but low levels of trimeric and tetrameric species were also detectable. These data are consistent with the proposal that, during assembly of intact protein molecules into IF, the headpiece and Helix 1 contribute to dimerization of two polypeptides into a parallel, in-register coiled-coil. However, additional interactions, including headpiece-to-rod binding and hydrophobic interaction along the entire rod domain, are required to stabilize the tetramers and full-size IF.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Saeed T,Ip W

doi

10.1016/0006-291x(89)92709-5

subject

Has Abstract

pub_date

1989-12-29 00:00:00

pages

1059-66

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)92709-5

journal_volume

165

pub_type

杂志文章

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