| Literature DB >> 8950169 |
K Menz1, N Radomski, E Jost.
Abstract
An important step in understanding nuclear structure and its function in replication and gene regulation is the cloning and characterisation of nuclear matrix proteins. A full-length cDNA-clone, encoding a novel nuclear matrix protein, was isolated from a (lambda gt11 cDNA library derived from murine macrophages. The antibody used for the screen was raised against a single polypeptide isolated from two-dimensional gel electrophoresis of nuclear matrix preparations. The cDNA encodes a protein of 446 amino acids named INMP for intranuclear matrix protein. INMP displays several salient features, a coiled-coil domain, a leucine zipper, a number of phosphorylation sites and a putative nuclear localisation signal. Sequence homology comparisons indicate that INMP is a unique protein which is evolutionary related to the gene family of intermediate filament-like proteins, especially the nuclear lamins.Entities:
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Year: 1996 PMID: 8950169 DOI: 10.1016/s0167-4781(96)00132-7
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002