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Reassembling proteins and chaperones in human nuclear matrix protein fractions

✍ Scribed by Christopher Gerner; Klaus Holzmann; Michael Meissner; Josef Gotzmann; Rudolf Grimm; Georg Sauermann

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 225 KB
Volume: 74
Category: Article
ISSN: 0730-2312
DOI: 10.1002/(sici)1097-4644(19990801)74:2<145::aid-jcb1>3.0.co;2-#

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✦ Synopsis

To detect putative filament forming components, nuclear matrix proteins were searched for proteins extensively reassembling from urea solution. Eight proteins, ubiquitously occurring in various human cell types, but not apparent in the cytosol, were registered by means of two-dimensional gel electrophoresis. They consisted of a protein exhibiting a novel amino acid sequence; of nuclear lamin B2, RbAp46, and RbAp48; and of four as yet unknown proteins. Furthermore, partial sequencing, mass spectrometry, and immunodetection of proteins demonstrated the presence of molecular chaperones and protein folding catalysts in the nuclear matrix fractions. In addition to a TCP-1-related protein, certain members of the heat shock, PDI, and calreticulin family of proteins were detected. On the basis of the absence of several other heat shock proteins in the nuclear matrix fraction, a general contamination by cytoplasmic chaperones appears unlikely.

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