A Tudor protein with multiple SNc domains from pea seedlings : cellular localization, partial characterization, sequence analysis, and phylogenetic relationships

A major high molecular weight protein (HMP) in the cytoskeletal fraction from pea has been purified. A combination of chromatographic techniques and protease fragment analysis also facilitated the isolation of the encoding cDNA, disclosing the sequence of the complete open reading frame. The protein...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 54(2003), 384 vom: 26. März, Seite 971-83
1. Verfasser: Abe, Shunnosuke (VerfasserIn)
Weitere Verfasser: Sakai, Masako, Yagi, Kosaku, Hagino, Takehiko, Ochi, Katsumasa, Shibata, Koichi, Davies, Eric
Format: Aufsatz
Sprache:English
Veröffentlicht: 2003
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cytoskeletal Proteins DNA, Complementary Plant Proteins RNA-Binding Proteins Micrococcal Nuclease EC 3.1.31.1
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245 1 2 |a A Tudor protein with multiple SNc domains from pea seedlings  |b cellular localization, partial characterization, sequence analysis, and phylogenetic relationships 
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520 |a A major high molecular weight protein (HMP) in the cytoskeletal fraction from pea has been purified. A combination of chromatographic techniques and protease fragment analysis also facilitated the isolation of the encoding cDNA, disclosing the sequence of the complete open reading frame. The protein possesses four complete N-terminal Staphylococcal nuclease (SNc) domains, a central Tudor domain and a partial SNc domain at the C-terminus, which may act as a coiled-coil cytoskeleton interaction motif. Cell fractionation studies showed that the protein was abundant in the cytoskeleton fraction in dark-grown pea seedlings, but essentially was absent from the nucleus. Gel filtration column chromatography indicated that the native protein exists as a dimer, while isoelectric focusing suggested that there were at least four HMP isotypes. The protein co-eluted with ribosomes from a heparin affinity column in vitro, consistent with ribosome/polysome interactions in vivo. Significantly, sequence analysis of the C-terminal SNc motif may accurately predict nuclear versus cytoplasmic localization resulting in potentially very different functional roles for this protein family in different organisms. An antibody to HMP from peas was also raised and an HMP with a similar molecular mass was detected in the cytoskeleton fractions and to a lesser extent in the nuclear fraction (250 g pellet) from rice and wheat seedlings 
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650 7 |a DNA, Complementary  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a RNA-Binding Proteins  |2 NLM 
650 7 |a Micrococcal Nuclease  |2 NLM 
650 7 |a EC 3.1.31.1  |2 NLM 
700 1 |a Sakai, Masako  |e verfasserin  |4 aut 
700 1 |a Yagi, Kosaku  |e verfasserin  |4 aut 
700 1 |a Hagino, Takehiko  |e verfasserin  |4 aut 
700 1 |a Ochi, Katsumasa  |e verfasserin  |4 aut 
700 1 |a Shibata, Koichi  |e verfasserin  |4 aut 
700 1 |a Davies, Eric  |e verfasserin  |4 aut 
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