The nuclear pore complex

Heese-Peck, Antje; Raikhel, Natasha V.

doi:10.1007/978-94-011-5298-3_8

Cited by 15 publications

(24 citation statements)

References 131 publications

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Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

“…Electron microscopy of NPCs has shown cytoplasmic as well as nuclear fibrils connected to the central pore complex, and it has been suggested that these peripheral structures connect nucleoplasmic and cytoplasmic cytoskeletal elements (Davis, 1995;Heese-Peck and Raikhel, 1998). Several NPC proteins from vertebrates and yeast contain ␣ -helical coiled-coil domains, which might allow them either to form the filamentous structures of the NPC or to associate with the structural proteins forming them (Heese-Peck and Raikhel, 1998).…”

Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

“…Several NPC proteins from vertebrates and yeast contain ␣ -helical coiled-coil domains, which might allow them either to form the filamentous structures of the NPC or to associate with the structural proteins forming them (Heese-Peck and Raikhel, 1998). Some of the yeast and vertebrate NPC proteins have structures that should allow them to bind to DNA or RNA.…”

Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

“…Animal and yeast nuclear pore complexes (NPCs) consist of ‫ف‬ 100 different proteins, of which only 25 to 30% are known (Heese-Peck and Raikhel, 1998). No plant genes encoding NPC proteins have been cloned, and no proteins with sequence similarity to the vertebrate and yeast NPC proteins have been found in plant databases, although candidate glycoproteins localized at the nuclear periphery have been identified recently (HeesePeck and Raikhel, 1998).Electron microscopy of NPCs has shown cytoplasmic as well as nuclear fibrils connected to the central pore complex, and it has been suggested that these peripheral structures connect nucleoplasmic and cytoplasmic cytoskeletal elements (Davis, 1995;Heese-Peck and Raikhel, 1998). Several NPC proteins from vertebrates and yeast contain ␣ -helical coiled-coil domains, which might allow them either to form the filamentous structures of the NPC or to associate with the structural proteins forming them (Heese-Peck and Raikhel, 1998).…”

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confidence: 99%

“…Vertebrate Nup153p contains several zinc fingers and has been shown to bind to Escherichia coli DNA in an in vitro gel blot assay (Sukegawa and Blobel, 1993). In addition, three known NPC proteins are transmembrane proteins (Heese-Peck and Raikhel, 1998) and are believed to be involved in anchoring the NPC to the membranes of the nuclear envelope.A protein like MFP1, possessing a membrane-attachment domain, filament protein structure, as well as the ability to specifically bind to DNA, is an interesting candidate for a plant NPC-associated protein. Whereas NPCs appear somewhat too small and too abundant, as shown by using electron microscopy, to account for the MFP1-associated speckles, the localization of a protein containing a plant nuclear localization signal to isolated tobacco nuclei shows a pattern of speckles of ‫ف‬ 0.5 m in diameter, which is strikingly similar to the localization pattern of MFP1 (Hicks et al, 1996).…”

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confidence: 99%

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Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Gindullis

Meier

1999

Plant Cell

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Recently, it has been suggested that nuclear processes, such as replication, transcription, and splicing, are spatially organized and associated with a nuclear framework called the nuclear matrix, a structure of unknown molecular composition. It has been shown that chromatin is attached to the nuclear matrix via specific DNA fragments called matrix attachment regions (MARs). We have begun to dissect the plant nuclear matrix by isolating a DNA binding protein with specific affinity for MARs. Here, it is shown that MAR binding filament-like protein 1 (MFP1) is associated with specklelike structures at the nuclear periphery that are part of isolated nuclei and the nuclear matrix. A predicted N-terminal transmembrane domain is necessary for the specific targeting of MFP1 to the speckles, indicating an association with the nuclear envelope-endoplasmic reticulum continuum. In addition, it is shown that a marker protein for plant microtubule organizing centers, which has been shown to be localized on the outside of the plant nuclear envelope, is also part of the nuclear matrix. These findings indicate a close and previously undescribed connection in plants between the nuclear envelope and the internal nuclear matrix, and they suggest a function for MFP1 in attaching chromatin to specific sites at the nuclear periphery. INTRODUCTIONThe nuclear matrix hypothesis proposes a structural framework for the eukaryotic nucleus that is similar to the cytoskeleton. Biochemically, the nuclear matrix is defined as the insoluble material that remains after extraction of nuclei with high-salt solutions (Berezney and Coffey, 1974) or with the chaotropic agent lithium diiodosalicylate (Mirkovitch et al., 1984) and treatment with DNases. Electron microscopy has shown a network of fibers of ‫ف‬ 10 nm in diameter. These fibers resemble the intermediate filaments of the cytoskeleton. Because they can be detected only under certain preparation conditions (He et al., 1990), their in vivo existence has been somewhat controversial.The isolated nuclear matrix binds specifically to certain DNA elements called matrix attachment regions (MARs). MARs are generally AT-rich DNA sequences that are several hundred base pairs long and are localized in the noncoding regions of the DNA, often flanking genes (Gasser and Laemmli, 1987). MARs have a positive effect on gene expression (Allen et al., 1993(Allen et al., , 1996Mlynárová et al., 1996) that is believed to be due to the establishment of independent and transcriptionally active chromatin domains between two MARs (Spiker and Thompson, 1996). Although the nuclear matrix was identified more than 20 years ago (Berezney and Coffey, 1974), none of its structural components has been isolated and molecularly characterized from any organism. One strategy to identify such components has been to isolate proteins that specifically bind to MARs. A small number of MAR binding proteins have been purified and cloned from animals, and they subsequently have been shown to be localized in the nuclear matrix (von Kri...

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Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

Section: Mfp1 and The Plant Nuclear Envelope-er Continuummentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Gindullis

Meier

1999

Plant Cell

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Two birds with one stone: genes that encode products targeted to two or more compartments

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Wintz

Akashi

et al. 1998

Protein Trafficking in Plant Cells

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The plant nuclear envelope

Meier¹

2001

CMLS, Cell. Mol. Life Sci.

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This review summarizes our present knowledge about the composition and function of the plant nuclear envelope. Compared with animals or yeast, our molecular knowledge of the nuclear envelope in higher plants is in its infancy. However, there are fundamental differences between plants and animals in the structure and function of the nuclear envelope. This review will compare and contrast these differences for nuclear pore complexes, nuclear transport, inner nuclear envelope proteins and the role of the nuclear envelope during mitosis. In some cases, seemingly 'novel' aspects of plant nuclear envelope function may provide new insight into the animal cell nucleus.

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The nuclear pore complex

Cited by 15 publications

References 131 publications

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Matrix Attachment Region Binding Protein MFP1 Is Localized in Discrete Domains at the Nuclear Envelope

Two birds with one stone: genes that encode products targeted to two or more compartments

The plant nuclear envelope

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