Abstract:
:The polymerization of scallop beta-like actin is significantly slower than that of skeletal muscle alpha-actin. To reveal which steps of polymerization contribute to this difference, we estimated the efficiency of nucleation of the two actins, the rates of filament elongation at spontaneous and gelsolin-nucleated polymerization and the turnover rates of the filament subunits at steady-state. Scallop actin nucleated nearly twice less efficient than rabbit actin. In actin filaments with free ends, when dynamics at the barbed ends overrides that at the pointed ends, the relative association rate constants of alpha- and beta-actin were similar, whereas the relative dissociation rate constant of beta-ATP-actin subunits was 2- to 3-fold higher than that of alpha-actin. The 2- to 3-fold faster polymerization of skeletal muscle versus scallop Ca-actin was preserved with gelsolin-capped actin filaments when only polymerization at the pointed end is possible. With gelsolin-induced polymerization, the rate constants of dissociation of ATP-actin subunits from the pointed ends were similar, while the association rate constant of beta-actin to the pointed filament ends was twice lower than that of alpha-actin. This difference may be of physiological relevance for functional intracellular sorting of actin isoforms.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Khaitlina S,Hinssen Hdoi
10.1016/j.abb.2008.06.016subject
Has Abstractpub_date
2008-09-15 00:00:00pages
279-84issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(08)00316-0journal_volume
477pub_type
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1993-10-01 00:00:00
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pub_type: 杂志文章
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更新日期:1987-11-01 00:00:00
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更新日期:1987-11-01 00:00:00