A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
Article Abstract:
A nucleoporin (nup) was isolated from extracts of rat liver nuclear envelope using monoclonal antibodies raised against repetitive motifs present in previously characterized nups. The gene coding for the new nup, designated nup153, was isolated and characterized. Sequence analysis showed that nup153 contains four repeats of a zinc finger motif. In addition, the nup was localized to the nucleoplasmic side of the nuclear pore complex. These results indicate that nup153 is able to bind to specific DNA sequences and is involved in gene-gating and genome organizing functions.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation
Article Abstract:
In vitro analysis was employed to evaluate the influence of lumenal contents of the endoplasmic reticulum in protein translocation. There were two stages of the translocation process involving the depletion of the reticuloplasm. The first stage did not record any response to the depletion of the reticuloplasm, but the second showed change. The study proved that lumenal proteins are essential in the mammalian endoplasmic reticulum for the purposes of protein translocation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha
Article Abstract:
A study was conducted to characterize the crystal structures of the arm-repeat region of Saccharomyces cerevisiae karyopherin in unliganded form and in complex with a peptide. Multiple isomorphous replacement was carried out to determine structure phases. Results indicated that the repeated arm motifs support a complex set of interactions with the backbone and side chains of the nuclear localization signals.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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