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Reassembling proteins and chaperones in human nuclear matrix protein fractions
Author(s) -
Gerner Christopher,
Holzmann Klaus,
Meissner Michael,
Gotzmann Josef,
Grimm Rudolf,
Sauermann Georg
Publication year - 1999
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19990801)74:2<145::aid-jcb1>3.0.co;2-#
Subject(s) - nuclear matrix , heat shock protein , nuclear lamina , cytoplasm , cytosol , biochemistry , nuclear protein , calreticulin , chemistry , gel electrophoresis , protein folding , chaperone (clinical) , biology , endoplasmic reticulum , gene , chromatin , medicine , pathology , transcription factor , enzyme
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. J. Cell. Biochem. 74:145–151, 1999. © 1999 Wiley‐Liss, Inc.