Qq. Li et al., A NOVEL CELL-CYCLE-DEPENDENT 350-KDA NUCLEAR-PROTEIN - C-TERMINAL DOMAIN SUFFICIENT FOR NUCLEAR-LOCALIZATION, Biochemical and biophysical research communications, 212(1), 1995, pp. 220-228
We have screened human scleroderma patients for immunoreactivity with
the components of the nucleus and the mitotic apparatus. We announce t
he identification of a novel cell-cycle-dependent nuclear protein usin
g serum from a CREST patient AH. AH protein first appears at the nucle
us 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 progressivel
y disperses from the kinetochore and becomes diffusely localized in th
e cytoplasm and in telophase; it appears to be enriched within the int
racellular bridge. Molecular cloning and transfection studies reveal t
hat the 350-kDa AH protein contains a coiled-coil and a globular domai
n at the C-terminus that is sufficient for nuclear localization. (C) 1
995 Academic Press, Inc.