Identification of a Protein which Specifically Binds a Highly Repetitive Heterochromatic DNA Family (Alu 1 Family) of Artemia Franciscana
Part of the
NATO ASI Series
book series (NSSA, volume 174)
Heterochromatin, the most highly condensed region of interphase chromosomes and generally located in centromeric and telomeric regions, contains nucleotide sequences of length from about 10 to more than 103 base pairs repeated thousands to millions of times per haploid genome and arranged in long tandem arrays (satellite DNA) [1–5]. Even if the sequences of the heterochromatic DNA are assumed to be the primary cause of differential condensation, other chromosomal constituents, such as proteins and RNA, must mediate this folding [6,7]. Therefore, the understanding of the molecular mechanisms involved in heterochromatin condensation requires knowledge of heterochromatic DNA sequence organization as well as identification of proteins with the potential role to maintain higher order heterochromatin structure.
KeywordsInterphase Nucleus Nitrocellulose Filter Specific Binding Activity Immune Rabbit Serum Phosphocellulose Column
W. J. Peacock, A. R. Lohe, W. L. Gerlach, P. Dunsmuir, E. S. Dennis and R. Appels, “Fine structure and evolution of DNA in Heterochromatin,” Cold Spring Harbor Symp. Quant. Biol.
42:1121 (1977).CrossRefGoogle Scholar
B. John and G. L. C. Miklas, Functional aspects of satellite DNA and heterochromatin, Int. Rev. Cytol.
58:1 (1979).PubMedCrossRefGoogle Scholar
D. L. Brutlag, Molecular arrangement and evolution of heterochromatic DNA, Ann. Rev. Genet.
14:121 (1980).PubMedCrossRefGoogle Scholar
M. F. Singer, Highly repeated sequences in mammalian genomes, Int. Rev. Cytol.
76:67 (1982).PubMedCrossRefGoogle Scholar
M. Gatty, D. A. Smith and B. S. Baker, A gene controlling condensation of heterochromatin in Drosophila melanagaster
221:83 (1983).CrossRefGoogle Scholar
T. Hsieh and D. L. Brutlag, A protein that preferentially binds Drosophila
satellite DNA, Proc. Natl. Acad. Sci.
U.S.A. 76:726 (1979).PubMedCrossRefGoogle Scholar
C. R. Rodriguez-Alfageme, G. T. Rudkin and L. H. Cohen, Isolation, properties and cellular distribution of Dl, a chromosomal protein of Drosophila
(Berl.) 78:1 (1980).CrossRefGoogle Scholar
C. R. Rodriguez-Alfageme, G. T. Rudkin and L. H. Cohen, Locations of chromosomal proteins in polytene chromosomes, Proc. Natl. Acad. Sci.
U.S.A. 73:2038 (1976)CrossRefGoogle Scholar
L. Levinger and A. Varshavsky, Protein Dl preferentially binds A + T-rich DNA in vitro
and is a component of Drosophila melanogaster
nucleosomes containing A + T-rich satellite DNA, Proc. Natl. Acad. Sci.
U.S.A. 79:7152 (1982).PubMedCrossRefGoogle Scholar
F. C. Bennet, B. I. Rosenfeld, C. K. Huang and L. C. Yeoman, Evidence for two conformational forms of nonhistone protein BA which differ in their affinity for DNA, Biochem. Biophys. Res. Commun.
104:649 (1982).CrossRefGoogle Scholar
F. Strauss and A. Varshavsky, A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome, Cell
37:889 (1984).PubMedCrossRefGoogle Scholar
M. J. Solomon, F. Strauss and A. Varshavsky, A mammalian high mobility group protein recognizes any Stretch of six A-T base pairs in duplex DNA, Proc. Natl. Acad. Sci.
U.S.A. 83:1276 (1986).PubMedCrossRefGoogle Scholar
C. Barigozzi, G. Badaracco, P. Plevani, L. Baratelli, S. Profeta, E. Ginelli and R. Meneveri, Heterochromatin in the genus Artemia
(Berl.) 90:332 (1984).CrossRefGoogle Scholar
G. Badaracco, L. Baratelli, E. Ginelli, R. Meneveri, P. Plevani, P. Valsasnini and C. Barigozzi, Variations in repetitive DNA and heterochromatin in the genes Artemia
(Berl.) 95:71 (1987).CrossRefGoogle Scholar
M. M. Garner and A. Revzin, A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: Application to components of the Escherichia coli
lactose operon regulatory system, Nucl. Acids Res.
9:3047 (1981).PubMedCrossRefGoogle Scholar
R. Maniatis, E. F. Fritsch and J. Sambrook, “Molecular Cloning: A Laboratory Manual,” Cold Spring Harbor Press, Cold Spring Harbor (1982).Google Scholar
U. K. Laemmli and M. Favre, Maturation of the head of bacteriophage T4. 1. DNA packaging events, J. Mol. Biol.
80:575 (1973).PubMedCrossRefGoogle Scholar
P. Plevani, G. Badaracco, C. Angl and L. M. S. Chang, DNA Polymerase I and DNA primase complex in yeast, J. Biol. Chem.
259:7532 (1984).PubMedGoogle Scholar
J. L. Vaitukatis, Production of antisera with small doses of immunogen: multiple intradermal injection, Methods in Enzymology 73:46 (1981).CrossRefGoogle Scholar
S. N. Hsu, L. Daine and H. Fanger, Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures, Jour. Histochem. Cytochem.
29:577 (1981).CrossRefGoogle Scholar
R. S. Jack, M. T. Brown and W. J. Gehsuing, Protein blotting as a means to detect sequence-specific DNA-binding proteins, Cold Spring Harbor Symp. Quant. Biol.
XLVII:483 (1982).Google Scholar
J. Cruces, M. L. G. Wonenburger, M. Diaz-Guerra, J. Sebastian and J. Renart, Satellite DNA in the crustacean Artemia
44:341 (1986).PubMedCrossRefGoogle Scholar
© Plenum Press, New York 1989