Lamin-like analogues in plants : the characterization of NMCP1 in Allium cepa

The nucleoskeleton of plants contains a peripheral lamina (also called plamina) and, even though lamins are absent in plants, their roles are still fulfilled in plant nuclei. One of the most intriguing topics in plant biology concerns the identity of lamin protein analogues in plants. Good candidate...

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Détails bibliographiques
Publié dans:Journal of experimental botany. - 1985. - 64(2013), 6 vom: 01. Apr., Seite 1553-64
Auteur principal: Ciska, Malgorzata (Auteur)
Autres auteurs: Masuda, Kiyoshi, Moreno Díaz de la Espina, Susana
Format: Article en ligne
Langue:English
Publié: 2013
Accès à la collection:Journal of experimental botany
Sujets:Journal Article Research Support, Non-U.S. Gov't Nuclear Proteins Plant Proteins
Description
Résumé:The nucleoskeleton of plants contains a peripheral lamina (also called plamina) and, even though lamins are absent in plants, their roles are still fulfilled in plant nuclei. One of the most intriguing topics in plant biology concerns the identity of lamin protein analogues in plants. Good candidates to play lamin functions in plants are the members of the NMCP (nuclear matrix constituent protein) family, which exhibit the typical tripartite structure of lamins. This paper describes a bioinformatics analysis and classification of the NMCP family based on phylogenetic relationships, sequence similarity and the distribution of conserved regions in 76 homologues. In addition, NMCP1 in the monocot Allium cepa characterized by its sequence and structure, biochemical properties, and subnuclear distribution and alterations in its expression throughout the root were identified. The results demonstrate that these proteins exhibit many similarities to lamins (structural organization, conserved regions, subnuclear distribution, and solubility) and that they may fulfil the functions of lamins in plants. These findings significantly advance understanding of the structural proteins of the plant lamina and nucleoskeleton and provide a basis for further investigation of the protein networks forming these structures
Description:Date Completed 24.09.2013
Date Revised 21.10.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/ert020