Protein-protein and protein-chromatin interactions at the nuclear envelope.
Item
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Title
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Protein-protein and protein-chromatin interactions at the nuclear envelope.
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Identifier
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AAI9630529
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identifier
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9630529
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Creator
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Ye, Qian.
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Contributor
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Adviser: Howard J. Worman
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Date
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1996
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Cell | Biology, Molecular
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Abstract
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The nuclear envelope consists of the nuclear membranes, the nuclear pore complexes and the nuclear lamina. I determined the primary structure of human lamin B receptor (LBR), an integral protein of the nuclear inner membrane. Human LBR has a basic nucleoplasmic amino-terminal domain of 208 amino acids followed by a hydrophobic domain of 407 amino acids that consist of eight putative transmembrane segments. The amino-terminal domain of human LBR can bind B-type lamins and double-stranded DNA in vitro. Two human proteins homologous to a Drosophila heterochromatin HP1, termed Hp1{dollar}\rm\sp{lcub}Hs\alpha{rcub}{dollar} and HP1{dollar}\rm\sp{lcub}HS\gamma{rcub},{dollar} were shown to interact with LBR amino-terminal domain in vitro and in vivo. Drosophila HP1 is important for the maintenance and formation of heterochromatin, which is partially associated with the periphery of nuclear envelope. The interactions of LBR with DNA and heterochromatin proteins may mediate the association of the heterochromatin with the inner nuclear membrane and may play a role in packaging chromatin into transcriptionally inactive domains. The interaction of LBR with B-type lamins can mediate the anchoring of the nuclear lamina to the inner nuclear membrane. I also used the yeast two-hybrid system to examine the interactions between the predominant human nuclear lamins including lamin A, lamin B1, lamin C and lamin A precursor prelamin A. All of these four lamin proteins are able to form homodimers as well as heterodimers. This result suggests when multiple lamins are expressed in the cells, the nuclear lamina can potentially consist of homotypic and heterotypic lamin filaments.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
