Interaction of plant polysomes with the actin cytoskeleton.

Abstract:

:Protein composition and functional activity of various polysome subpopulations isolated from Vicia faba L. leaves and Triticum aestivum L. and Hordeum vulgare L. seedlings were studied. Membrane- and cytoskeleton-bound polysomes were more active in the wheat germ cell-free translational system than free polysomes. Several non-ribosomal proteins were detected in the polysome preparations by gel electrophoresis and Western blot analysis: (1) a canonical actin of mol wt 42 kDa; (2) a 40 kDa protein, demonstrating affinity for ribosomes, sharing some determinants with actin, and present predominantly in the subpopulations of bound polysomes; and (3) an acidic ribosome-associated p40 evenly distributed between free and bound polysomes. The possibility of involvement of these proteins in interactions between polysomes and the actin cytoskeleton is discussed.

journal_name

Cell Biol Int

authors

Klyachko N,Aksenova L,Dunaeva M,Kulikova A

doi

10.1006/cbir.1999.0517

keywords:

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

351-8

issue

6

eissn

1065-6995

issn

1095-8355

pii

S1065-6995(99)90517-6

journal_volume

24

pub_type

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