Synthesis and stability of nuclear matrix proteins in resting and serum‐stimulated swiss 3T3 cells

Milavetz, Barry; Edwards, Dylan R.

doi:10.1002/jcp.1041270306

Cited by 5 publications

(2 citation statements)

References 29 publications

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“…The 2D analyses of nuclear matrix proteins performed by several groups stress the high degree of complexity of these polypeptide profiles (13,(40)(41)(42)(43)(44)(45)(46). By using [35S]methionine labeling for detection, Fey and Penman (42) have detected >200 proteins in the nuclear matrix.…”

Section: Discussionmentioning

confidence: 99%

“…The remaining eight major proteins termed the nuclear matrins consisted of matrin 3 (125 kDa, slightly acidic), matrin 4 (105 kDa, basic), matrins D-G (60-75 kDa, basic), and matrins 12 and 13 (42)(43)(44)(45)(46)(47)(48)acidic). Peptide mapping and two-dimensional immunoblot studies indicate that matrins D-G compose two pairs of related proteins (matrins D/E and F/G) and that none of the matrins resemble the nuclear lamins or any of the other major proteins detected on our two-dimensional gels.…”

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confidence: 99%

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Nuclear matrins: identification of the major nuclear matrix proteins.

Nakayasu

Berezney

1991

Proc. Natl. Acad. Sci. U.S.A.

182

115

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A preparative two-dimensional polyacrylamide gel system was used to separate and purify the majorCoomassie blue-stained proteins from the isolated rat liver nuclear matrix. Approximately 12 major proteins were consistently found. Of these, 5 proteins represented identified proteins, including nuclear lamins A, B, and C, the nucleolar protein B-23, and residual components of core heterogeneous nuclear ribonucleoproteins. The remaining eight major proteins termed the nuclear matrins consisted of matrin 3 (125 kDa, slightly acidic), matrin 4 (105 kDa, basic), matrins D-G (60-75 kDa, basic), and matrins 12 and 13 (42-48 kDa, acidic). Peptide mapping and two-dimensional immunoblot studies indicate that matrins D-G compose two pairs of related proteins (matrins D/E and F/G) and that none of the matrins resemble the nuclear lamins or any of the other major proteins detected on our two-dimensional gels. Subfractionation immunoblot experiments demonstrated the nearly exclusive localization of matrins F/G and other matrins to the nuclear matrix fraction of the cell. These results were further supported by indirect immunofluorescence microscopy that showed a strictly interior nuclear localization of the matrins in intact cells in contrast to the peripherally located nuclear lamins. We conclude that the nuclear matrins are a major class of proteins of the nuclear matrix interior and are distinct from the nuclear lamins.There is a growing awareness that many of the important answers to questions concerning the expression and regulation of the eukaryotic genome will require an understanding of the higher-order arrangement and function of the genetic components as they interact within the complex threedimensional architecture of the cell nucleus (1-13). The nuclear matrix, a residual nuclear structure that has been isolated from a wide variety of eukaryotic cells throughout the phylogenetic scale (1-3, 6, 7, 13-16), offers a potentially valuable in vitro approach for studying nuclear processes in relation to nuclear structure. Indeed, numerous studies have implicated the matrix as a site of organization for virtually all known nuclear processes (1-11, 13, 16), such as, DNA loop attachment, DNA replication, transcription, RNA splicing and transport, hormone receptor function, carcinogen binding, oncogene proteins, viral proteins, and protein phosphorylation. Despite this progress, our knowledge of the proteins that compose this proteinaceous nucleoskeletal structure is still in its infancy. In this study we have used high-resolution preparative PAGE to identify and purify many of the major Coomassie blue-stained nuclear matrix proteins. A class of nuclear matrix proteins termed the nuclear matrins is identified and characterized by peptide maps, polyclonal antibodies generated against the individual purified matrins, and indirect immunofluorescence microscopy.

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