Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Blumenthal, Sonal S. D.; Clark, Gregory B.; Roux, Stanley J.

doi:10.1007/s00425-003-1182-5

Cited by 34 publications

(7 citation statements)

References 47 publications

(53 reference statements)

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“…In other monocots such as wheat and rye and also garlic that belongs to the genus Allium , the antibody cross-reacted with proteins of 100kDa, while in maize the antibody recognized a triplet of about 80kDa. In pea, a major band of a similar size (70kDa) to a protein of the peripheral nuclear matrix described previously (Blumenthal et al ., 2004) was detected. The diversity of molecular weights across species may indicate that NMCPs undergo alternative splicing and/or post-translational modifications.…”

Section: Resultssupporting

confidence: 58%

“…These proteins probably share some structural properties of lamins that are essential for their activity rather than specific sequence homology. Early studies of the plant NSK described proteins that are immunologically related to lamins and IFs, with similar molecular weights, pI, solubility, and nuclear distribution in both monocots and dicots (Blumenthal et al ., 2004; Moreno Díaz de la Espina, 2009). However, no full sequence has been ascribed to these proteins to date.…”

Section: Introductionmentioning

confidence: 99%

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

Ciska¹,

Masuda

Espina³

2013

Journal of Experimental Botany

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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.

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Section: Resultssupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

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

Ciska¹,

Masuda

Espina³

2013

Journal of Experimental Botany

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“…Well defined tightly packed filaments were observed at the INM of tobacco cells, suggesting that the lamina would be formed by proteins that can form filaments ( Figure 2C ). The filaments in the lamina were 10–13 or 5–8 nm thick, similar dimensions to those observed in isolated lamina fractions from pea nuclei (Li and Roux, 1992; Blumenthal et al, 2004; Fiserova et al, 2009). On view of the structural similarities of the metazoan and plant lamina, the specific term plamina recently coined for the plant lamina is not necessary, adds confusion to the field and should be avoided.…”

Section: The Plant Laminasupporting

confidence: 72%

“…Since the discovery of the plant lamina several insoluble proteins have been proposed as putative plant lamin-like proteins, mainly based on their localization in the lamina, their cross reactivity with vertebrate lamins and intermediate filaments (Li and Roux, 1992; Minguez and Moreno Diaz de la Espina, 1993; Moreno Diaz de la Espina, 1995, 2009), and on their ability to form filaments in vitro (Blumenthal et al, 2004). However, the sequences of these proteins are still not available to analyze and compare them with lamins.…”

Section: Protein Components Of the Plant Laminamentioning

confidence: 99%

The intriguing plant nuclear lamina

Ciska

Espina

2014

Front. Plant Sci.

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The nuclear lamina is a complex protein mesh attached to the inner nuclear membrane (INM), which is also associated with nuclear pore complexes. It provides mechanical support to the nucleus and nuclear envelope, and as well as facilitating the connection of the nucleoskeleton to the cytoskeleton, it is also involved in chromatin organization, gene regulation, and signaling. In metazoans, the nuclear lamina consists of a polymeric layer of lamins and other interacting proteins responsible for its association with the INM and chromatin. In plants, field emission scanning electron microscopy of nuclei, and thin section transmission electron microscopy of isolated nucleoskeletons, reveals the lamina to have a similar structure to that of metazoans. Moreover, although plants lack lamin genes and the genes encoding most lamin-binding proteins, the main functions of the lamina are fulfilled in plants. Hence, it would appear that the plant lamina is not based on lamins and that other proteins substitute for lamins in plant cells. The nuclear matrix constituent proteins are the best characterized structural proteins in the plant lamina. Although these proteins do not display strong sequence similarity to lamins, their predicted secondary structure and sub-nuclear distribution, as well as their influence on nuclear size and shape, and on heterochromatin organization, suggest they could be functional lamin analogs. In this review we shall summarize what is currently known about the organization and composition of the plant nuclear lamina and its interacting complexes, and we will discuss the activity of this structure in the plant cell and its nucleus.

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“…Nuclear intermediate filament proteins are immunologically identified candidates that form 6–12 nm, lamin-like filaments in vitro (24). Another group of candidates are the nuclear matrix constituent proteins at the nuclear periphery.…”

Section: Introductionmentioning

confidence: 99%

Co-dependence between trypanosome nuclear lamina components in nuclear stability and control of gene expression

et al. 2016

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The nuclear lamina is a filamentous structure subtending the nuclear envelope and required for chromatin organization, transcriptional regulation and maintaining nuclear structure. The trypanosomatid coiled-coil NUP-1 protein is a lamina component functionally analogous to lamins, the major lamina proteins of metazoa. There is little evidence for shared ancestry, suggesting the presence of a distinct lamina system in trypanosomes. To find additional trypanosomatid lamina components we identified NUP-1 interacting proteins by affinity capture and mass-spectrometry. Multiple components of the nuclear pore complex (NPC) and a second coiled-coil protein, which we termed NUP-2, were found. NUP-2 has a punctate distribution at the nuclear periphery throughout the cell cycle and is in close proximity to NUP-1, the NPCs and telomeric chromosomal regions. RNAi-mediated silencing of NUP-2 leads to severe proliferation defects, gross alterations to nuclear structure, chromosomal organization and nuclear envelope architecture. Further, transcription is altered at telomere-proximal variant surface glycoprotein (VSG) expression sites (ESs), suggesting a role in controlling ES expression, although NUP-2 silencing does not increase VSG switching. Transcriptome analysis suggests specific alterations to Pol I-dependent transcription. NUP-1 is mislocalized in NUP-2 knockdown cells and vice versa, implying that NUP-1 and NUP-2 form a co-dependent network and identifying NUP-2 as a second trypanosomatid nuclear lamina component.

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Biochemical and immunological characterization of pea nuclear intermediate filament proteins

Cited by 34 publications

References 47 publications

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

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

The intriguing plant nuclear lamina

Co-dependence between trypanosome nuclear lamina components in nuclear stability and control of gene expression

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