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Cell. 1993 Jan 15;72(1):29-38.

A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm.

Author information

1
Howard Hughes Medical Institute, Rockefeller University, Laboratory of Cell Biology, New York, New York 10021.

Abstract

We have molecularly cloned and sequenced a cDNA for a rat liver nucleoporin with a molecular mass of 152.8 kd, termed nup153, that shares a repetitive degenerate pentapeptide motif with a subgroup of nucleoporins of yeast and vertebrates. However, its most striking feature is a novel 4-fold repeat of a Cys2-Cys2-type zinc finger motif. When expressed in E. coli, the zinc finger domain of nup153 binds DNA in a zinc-dependent fashion. Immunoelectron microscopy localized nup153 exclusively to the nucleoplasmic side of the nuclear pore complex. We suggest that nup153 recognizes a specific DNA sequence to organize the genome three-dimensionally and to gate transcribable genes to nuclear pore complexes.

PMID:
8422679
[Indexed for MEDLINE]

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