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Biochem Biophys Res Commun. 1995 Jul 6;212(1):220-8.

A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain sufficient for nuclear localization.

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Graduate Program in Biochemistry and Molecular Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.


We have screened human scleroderma patients for immunoreactivity with the components of the nucleus and the mitotic apparatus. We announce the identification of a novel cell-cycle-dependent nuclear protein using serum from a CREST patient AH. AH protein first appears at the nucleus of G2-phase and associates with the centrosome throughout the cell cycle. As chromosomes condense during the prophase, AH protein becomes enriched at the kinetochores. During mitosis, AH protein progressively disperses from the kinetochore and becomes diffusely localized in the cytoplasm and in telophase; it appears to be enriched within the intracellular bridge. Molecular cloning and transfection studies reveal that the 350-kDa AH protein contains a coiled-coil and a globular domain at the C-terminus that is sufficient for nuclear localization.

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