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A high molecular weight polypeptide cross‐reacting with the antibodies to the dynein heavy chain localizes to the subset of Golgi complex in higher plant cells
Author(s) -
Shaniina A.,
Lazareva Elena M.,
Skorova Ekaterina Y.,
Chentsov Yuri S.,
Smirnova Elena A.
Publication year - 2009
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2008.12.004
Subject(s) - dynein , microtubule , golgi apparatus , phragmoplast , cell plate , microbiology and biotechnology , cytoplasm , dictyostelium discoideum , mitosis , biology , interphase , chemistry , cell division , biochemistry , spindle apparatus , cytokinesis , cell , endoplasmic reticulum , gene
Antibodies were produced against fragments of the microtubule‐binding domain and the motor domain of the dynein heavy chain from Dictyostelium discoideum to probe whole cell extracts of root meristem cells of wheat Triticum aestivum . In plant extracts, these antibodies cross‐reacted with a polypeptide of high molecular weight (>500 kDa). The antibodies bound to protein A‐Sepharose precipitated high molecular weight polypeptide from cell extracts. Immunofluorescence showed that the antibodies identified various aggregates inside cells, localized at the perinuclear area during interphase to early prophase, at the spindle periphery and polar area during mitosis, and in the interzonal region during phragmoplast development. Some aggregates were also co‐labeled by markers for the Golgi apparatus. Thus, we found in higher plant cells a high molecular weight antigen cross‐reacting with the antibodies to motor and microtubule‐binding domains of dynein heavy chains. This antigen is associated with aggregates distributed in the cytoplasm in cell cycle‐dependent manner. A subset of these aggregates belongs to the Golgi complex.