Highly conserved repetitive DNA sequences are present at human centromeres.

Grady, Deborah L.; Ratliff, Robert L.; Robinson, Donna L.; Mccanlies, Erin C.; Meyne, Julianne; Moyzis, Robert K.

doi:10.1073/pnas.89.5.1695

Cited by 185 publications

(142 citation statements)

References 29 publications

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“…These sequences are known to bind specific proteins which initiate the formation of a multiprotein complex (kinetochore) that binds to the ends of microtubules and helps in chromosomal migration during cell division [1]. Grady et al [2] have observed some proteins that bind specifically to the human centromeric repeat that we have studied. The dynamic base pairing scheme proposed above may play an important role in the specific protein recognition of this DNA repeat.…”

Section: Resultsmentioning

confidence: 97%

“…This repeat is also found on chromosomes that show high incidence of nondysjunction and other mitotic/meiotic abnormalities [3]. Grady et al [2] have shown recently that the purine strand of this sequence, (AATGN)n , forms a stable structure which likely incoporates G-A mismatched base pairs. In addition, this sequence behaved anomalously in gel electrophoresis.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

“…Their role in maintaining the structural integrity of chromosomes is evident. Human centromeric satellite DNA contains a highly conserved repeating sequence (AATGG)n" (CCATT)n [2]. This repeat is also found on chromosomes that show high incidence of nondysjunction and other mitotic/meiotic abnormalities [3].…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

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Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs

Jaishree

Wang

1994

FEBS Letters

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Nine DNA sequences related to the purine strand of the human centromeric satellite (AATGG)~.(CCATr)n repeat have been studied by two-dimensional nuclear magnetic resonance spectroscopy. Earlier studies have suggested that the structure of (AATGG)n sequence has an equilibrium between the duplex form and a fold-hack form. Structural refinement of d(CAATGG) and its related sequences by an NOE-constrained simulated annealing procedure reveals that the duplex form incorporates dynamic type-I G-A base pairs. 1D exchangeable proton NMR data support this model. The reverse sequence motif (GGTAA) destabilizes the structure.

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Section: Resultsmentioning

confidence: 97%

Section: Introduction 2 Materials and Methodsmentioning

confidence: 99%

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Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs

Jaishree

Wang

1994

FEBS Letters

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“…The formation of single-stranded DNA at heterochromatin blocks could originate from their characteristic enrichment on highly repetitive satellite DNA sequences, which is likely to promote strand slippage events during DNA replication. In this respect, the dodeca-satellite, like general satellites showing Pu-Py strand asymmetry, appear especially suited for the binding of DDP1 or vigilins in general, since its two strands show drastically different structural properties (6,7,13,14,27). The pyrimidine-rich strand could remain unstructured, providing long single-stranded DNA stretches, as required for efficient DDP1 binding.…”

Section: Resultsmentioning

confidence: 99%

“…In vitro, the dodeca-satellite can form altered DNA structures in which the G strand forms very stable intramolecular hairpins while the complementary C strand remains unstructured (13). Other centromeric satellites, such as the abundant Drosophila AAGAG satellite, show similar structural properties (6,7,14,27). Formation of these altered DNA structures could therefore provide an adequate substrate for the efficient binding of DDP1 to heterochromatin.…”

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confidence: 99%

DDP1, a Heterochromatin-Associated Multi-KH-Domain Protein of Drosophila melanogaster, Interacts Specifically with Centromeric Satellite DNA Sequences

Cortés

Azorı́n

2000

Molecular and Cellular Biology

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DDP1 is a single-stranded nucleic acid binding protein of Drosophila melanogaster that associates with pericentric heterochromatin. DDP1 contains 15 consecutive KH domains and is homologous to the highly conserved vigilin proteins that, in Saccharomyces cerevisiae, are involved in the control of cell ploidy. DDP1 was identified and purified on the basis of its binding to the pyrimidine-rich C strand of the centromeric Drosophila dodeca-satellite. Here, the interaction of DDP1 with the dodeca-satellite C strand was analyzed in detail. This interaction is sequence specific. In particular, a guanine residue which is highly conserved in natural dodecasatellite sequences was found to be essential for the efficient binding of DDP1. DDP1 binding was also found to be strongly influenced by the length and extent of secondary structure of the DNA substrate. Efficient DDP1 binding required a minimal length of about 75 to 100 nucleotides and was facilitated by the lack of secondary structure of the substrate. DDP1 also showed a significant affinity for the unstructured pyrimidine-rich strand of the most abundant centromeric Drosophila AAGAG satellite. The stoichiometry of the complexes formed with the dodeca-satellite C strand suggests that, in DDP1, the 15 consecutive KH domains are organized such that they define two nucleic acid binding surfaces. These results are discussed in the context of the possible contribution of DDP1 to heterochromatin organization and function.DDP1 is a multi-KH-domain protein of Drosophila melanogaster that is found associated with pericentric heterochromatin (8). DDP1 contains 15 tandemly organized KH domains and is homologous to the highly conserved vigilin proteins that have been found in all eukaryotic organisms analyzed to date, from yeasts to humans (25,29,30,38). Little is known about the functions of vigilins. They are up-regulated in rapidly dividing cells (29); in yeast, disruption of the corresponding gene (SCP160) results in cells with increased ploidy, suggesting a role in chromosome segregation (38). The expression of DDP1 complements a ⌬scp160 deletion in yeast (8). The association of DDP1 with pericentric heterochromatin also suggests a possible contribution to chromosome segregation. Vigilins could also play a role in RNA metabolism (12,17,(19)(20)(21). They were found to bind in vitro the 3Ј untranslated regions (UTRs) of the dystrophin and vitellogenin mRNAs and were proposed to be responsible for the increased stability of the latter induced by estrogens (12,17).Like the vigilins, DDP1 binds single-stranded nucleic acids with high affinity and specificity (8). Actually, DDP1 was identified and isolated on the basis of its interaction with the C strand of the Drosophila dodeca-satellite, a highly repeated DNA sequence which is localized to the pericentric heterochromatin on chromosome 3 in D. melanogaster (1,5,24). In polytene chromosomes, the distribution of DDP1 is not constrained to the regions containing dodeca-satellite sequences, being associated as well with other peri...

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Evolution of the centromeric alpha-satellite DNA sequences of human chromosome 22

Verma

1999

Prenat. Diagn.

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Highly conserved repetitive DNA sequences are present at human centromeres.

Cited by 185 publications

References 29 publications

Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs

Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs

DDP1, a Heterochromatin-Associated Multi-KH-Domain Protein of Drosophila melanogaster, Interacts Specifically with Centromeric Satellite DNA Sequences

Evolution of the centromeric alpha-satellite DNA sequences of human chromosome 22

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Highly conserved repetitive DNA sequences are present at human centromeres.

Cited by 185 publications

References 29 publications

Human chromosomal centromere (AATGG)n sequence forms stable structures with unusual base pairs

Human chromosomal centromere (AATGG)n sequence forms stable structures with unusual base pairs

DDP1, a Heterochromatin-Associated Multi-KH-Domain Protein of Drosophila melanogaster, Interacts Specifically with Centromeric Satellite DNA Sequences

Evolution of the centromeric alpha-satellite DNA sequences of human chromosome 22

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Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs

Human chromosomal centromere (AATGG)_n sequence forms stable structures with unusual base pairs