Satellite DNA sequences of Drosophila melanogaster

1975 ◽  
Vol 96 (4) ◽  
pp. 665-692 ◽  
Author(s):  
Sharyn A. Endow ◽  
Mary Lake Polan ◽  
Joseph G. Gall
Keyword(s):  
Drosophila Melanogaster ◽  
Dna Sequences ◽  
Satellite Dna

scholarly journals A DNA-binding protein from Ustilago maydis prefers duplex DNA without chain interruptions.

1983 ◽  
Vol 3 (4) ◽  
pp. 605-612 ◽  
Author(s):  
J R Rusche ◽  
W K Holloman
Keyword(s):  
Drosophila Melanogaster ◽  
Satellite Dna ◽  
Binding Assay ◽  
Ustilago Maydis ◽  
Dna Binding Protein ◽  
Double Strand Breaks ◽  
Duplex Dna ◽  
Plasmid Pbr322 ◽  
Strand Breaks ◽  
Dna Strand

Using a nitrocellulose filter binding assay, we have partially purified a protein from mitotic cells of Ustilago maydis that binds preferentially to covalently closed circular duplex DNA. DNA containing single- or double-strand breaks is bound poorly by the protein. Once formed, the DNA-protein complex is stable, resisting dissociation in high salt. However, when a DNA strand is broken, the complex appears to dissociate. The protein binds equally well to form I DNA of phi X174 or the plasmid pBR322, but has a higher affinity for a hybrid plasmid containing a cloned region of Drosophila melanogaster satellite DNA.

Restriction of P-element insertions at the Notch locus of Drosophila melanogaster

1987 ◽  
Vol 7 (4) ◽  
pp. 1545-1548
Author(s):  
M R Kelley ◽  
S Kidd ◽  
R L Berg ◽  
M W Young
Keyword(s):  
Drosophila Melanogaster ◽  
Dna Sequences ◽  
Consensus Sequence ◽  
P Element ◽  
Induced Mutations ◽  
P Elements ◽  
Target Dna ◽  
Complex Locus ◽  
Additional Level ◽  
Derivatives Of

P elements move about the Drosophila melanogaster genome in a nonrandom fashion, preferring some chromosomal targets for insertion over others (J. C. J. Eeken, F. H. Sobels, V. Hyland, and A. P. Schalet, Mutat. Res. 150:261-275, 1985; W. R. Engels, Annu. Rev. Genet. 17:315-344, 1983; M. D. Golubovsky, Y. N. Ivanov, and M. M. Green, Proc. Natl. Acad. Sci. USA 74:2973-2975, 1977; M. J. Simmons and J. K. Lim, Proc. Natl. Acad. Sci. USA 77:6042-6046, 1980). Some of this specificity may be due to recognition of a particular DNA sequence in the target DNA; derivatives of an 8-base-pair consensus sequence are occupied by these transposable elements at many different chromosomal locations (K. O'Hare and G. M. Rubin, Cell 34:25-36, 1983). An additional level of specificity of P-element insertions is described in this paper. Of 14 mutations induced in the complex locus Notch by hybrid dysgenesis, 13 involved P-element insertions at or near the transcription start site of the gene. This clustering was not seen in other transposable element-induced mutations of Notch. DNA sequences homologous to the previously described consensus target for P-element insertion are not preferentially located in this region of the locus. The choice of a chromosomal site for integration appears to be based on more subtle variations in chromosome structure that are probably associated with activation or expression of the target gene.

scholarly journals Transcription termination and processing of transcripts from tRNA-related Xenopus satellite DNA sequences

1987 ◽  
Vol 164 (2) ◽  
pp. 287-293 ◽  
Author(s):  
Wolfgang MEYERHOF ◽  
Burghardt WITTIG ◽  
Beatrix TAPPESER ◽  
Walter KNOCHEL
Keyword(s):  
Dna Sequences ◽  
Satellite Dna ◽  
Transcription Termination

Epigenetic control of mammalian centromere protein binding: does DNA methylation have a role?

1996 ◽  
Vol 109 (9) ◽  
pp. 2199-2206
Author(s):  
A.R. Mitchell ◽  
P. Jeppesen ◽  
L. Nicol ◽  
H. Morrison ◽  
D. Kipling
Keyword(s):  
Dna Sequences ◽  
Satellite Dna ◽  
Inbred Mouse ◽  
Inbred Mouse Strain ◽  
Chromosome 1 ◽  
Satellite Sequences ◽  
E Protein ◽  
Minor Satellite ◽  
Internal Block ◽  
Terminal Block

Chromosome 1 of the inbred mouse strain DBA/2 has a polymorphism associated with the minor satellite DNA at its centromere. The more terminal block of satellite DNA sequences on this chromosome acts as the centromere as shown by the binding of CREST ACA serum, anti-CENP-B and anti-CENP-E polyclonal sera. Demethylation of the minor satellite DNA sequences accomplished by growing cells in the presence of the drug 5-aza-2′-deoxycytidine results in a redistribution of the CENP-B protein. This protein now binds to an enlarged area on the more terminal block and in addition it now binds to the more internal block of minor satellite DNA sequences on chromosome 1. The binding of the CENP-E protein does not appear to be affected by demethylation of the minor satellite sequences. We present a model to explain these observations. This model may also indicate the mechanism by which the CENP-B protein recognises specific sites within the arrays of minor satellite DNA on mouse chromosomes.

Chromatin organization in the homogeneously staining regions of a methotrexate-resistant mouse cell line: interspersion of inactive and active chromatin domains distinguished by acetylation of histone H4

1996 ◽  
Vol 109 (9) ◽  
pp. 2221-2228 ◽  
Author(s):  
L. Nicol ◽  
P. Jeppesen
Keyword(s):  
Cell Line ◽  
Dna Sequences ◽  
Satellite Dna ◽  
Mouse Cell ◽  
Histone H4 ◽  
Active Chromatin ◽  
Chromatin Domains ◽  
Resistant Mouse ◽  
Major Satellite ◽  
Drosophila Heterochromatin

We have analyzed the organization of the homogeneously staining regions (HSRs) in chromosomes from a methotrexate-resistant mouse melanoma cell line. Fluorescence in situ hybridization techniques were used to localize satellite DNA sequences and the amplified copies of the dihydrofolate reductase (DHFR) gene that confer drug-resistance, in combination with immunofluorescence using antibody probes to differentiate chromatin structure. We show that the major DNA species contained in the HSRs is mouse major satellite, confirming previous reports, and that this is interspersed with DHFR DNA in an alternating tandem array that can be resolved at the cytological level. Mouse minor satellite DNA, which is normally located at centromeres, is also distributed along the HSRs, but does not appear to interfere with centromere function. The blocks of major satellite DNA are coincident with chromatin domains that are labelled by an autoantibody that recognizes a mammalian homologue of Drosophila heterochromatin-associated protein 1, shown previously to be confined to centric heterochromatin in mouse. An antiserum that specifically recognizes acetylated histone H4, a marker for active chromatin, fails to bind to the satellite DNA domains, but labels the intervening segments containing DHFR DNA. We can find no evidence for the spreading of the inactive chromatin domains into adjacent active chromatin, even after extended passaging of cells in the absence of methotrexate selection.

Sign in / Sign up

Export Citation Format

Share Document