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Book ; Thesis: A study of the error prone nature of primase from Escherichia coli

Bhattacharyya, Saumitri

the effect of DnaB Helicase

2000

Author's details	by Saumitri Bhattacharyya
Keywords	animal physiology
Language	English
Size	103 leaves ;, 28 cm.
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Thesis (Ph. D.)--University of Nebraska--Lincoln, 2000
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Article ; Online: Unwinding protein complexes in ALTernative telomere maintenance.

Bhattacharyya, Saumitri / Sandy, April / Groden, Joanna

Journal of cellular biochemistry

2009 Volume 109, Issue 1, Page(s) 7–15

Abstract: Telomeres are composed of specialized chromatin that includes DNA repair/recombination proteins, telomere DNA-binding proteins and a number of three dimensional nucleic acid structures including G-quartets and D-loops. A number of studies suggest that ... ...

Abstract	Telomeres are composed of specialized chromatin that includes DNA repair/recombination proteins, telomere DNA-binding proteins and a number of three dimensional nucleic acid structures including G-quartets and D-loops. A number of studies suggest that the BLM and WRN recQ-like helicases play important roles in recombination-mediated mechanisms of telomere elongation or Alternative Lengthening of Telomeres (ALT), processes that maintain/elongate telomeres in the absence of telomerase. BLM and WRN localize within ALT-associated nuclear bodies in telomerase-negative immortalized cell lines and interact with the telomere-specific proteins POT1, TRF1 and TRF2. Helicase activity is modulated by these interactions. BLM functions in DNA double-strand break repair processes such as non-homologous end joining, homologous recombination-mediated repair, resolution of stalled replication forks and synthesis-dependent strand annealing, although its precise functions at the telomeres are speculative. WRN also functions in DNA replication, recombination and repair, and in addition to its helicase domain, includes an exonuclease domain not found in other recQ-like helicases. The biochemical properties of BLM and WRN are, therefore, important in biological processes other than DNA replication, recombination and repair. In this review, we discuss some previous and recent findings of human rec-Q-like helicases and their role in telomere elongation during ALT processes.
MeSH term(s)	Animals ; Humans ; RecQ Helicases/physiology ; Telomere/chemistry ; Telomere/physiology ; Telomere-Binding Proteins/physiology
Chemical Substances	Telomere-Binding Proteins ; RecQ Helicases (EC 3.6.4.12)
Language	English
Publishing date	2009-11-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.22388
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Article: Srs2 helicase of Saccharomyces cerevisiae selectively unwinds triplet repeat DNA.

Bhattacharyya, Saumitri / Lahue, Robert S

The Journal of biological chemistry

2005 Volume 280, Issue 39, Page(s) 33311–33317

Abstract: ... expansions in vivo (Bhattacharyya, S., and Lahue, R. S. (2004) Mol. Cell. Biol. 24, 7324-7330). For example ...

Abstract	Trinucleotide repeat expansions are the mutational cause of at least 15 genetic diseases. In vitro, single-stranded triplet repeat DNA forms highly stable hairpins, depending on repeat sequence, and a strong correlation exists between hairpin-forming ability and the risk of expansion in vivo. Hairpins are viewed, therefore, as likely mutagenic precursors to expansions. If a helicase unwinds the hairpin, it would be less likely to expand. Previous work indicated that yeast Srs2 DNA helicase selectively blocks expansions in vivo (Bhattacharyya, S., and Lahue, R. S. (2004) Mol. Cell. Biol. 24, 7324-7330). For example, srs2 mutants, including an ATPase-defective point mutant, exhibit substantially higher expansion rates than wild type controls. In contrast, mutation of another helicase gene, SGS1, had little effect on expansion rates. These findings prompted the idea that Srs2 might selectively unwind triplet repeat hairpins. In this study, DNA helicase assays were performed with purified Srs2, Sgs1, and Escherichia coli UvrD (DNA helicase II). Srs2 shows substantially faster unwinding than Sgs1 or UvrD on partial duplex substrates containing (CTG) x (CTG) sequences, provided that Srs2 encounters the triplet repeat DNA immediately on entering the duplex. Srs2 was also faster at unwinding (CAG) x (CAG)- and (CCG) x (CCG)-containing substrates and an intramolecular (CTG) x (CTG) hairpin. In contrast, all three enzymes unwind about equally well control substrates with either Watson-Crick base pairs or mismatched substrates with non-CNG repeats. Overall, the selective unwinding activity of Srs2 on triplet repeat hairpin DNA helps explain the genetic evidence that Srs2, not the RecQ homolog Sgs1, is a preferred helicase for preventing expansions.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/isolation & purification ; Adenosine Triphosphatases/metabolism ; DNA/chemistry ; DNA/genetics ; DNA Helicases/genetics ; DNA Helicases/isolation & purification ; DNA Helicases/metabolism ; Escherichia coli Proteins ; Kinetics ; RecQ Helicases ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/isolation & purification ; Saccharomyces cerevisiae Proteins/metabolism ; Substrate Specificity ; Trinucleotide Repeat Expansion ; Trinucleotide Repeats
Chemical Substances	Escherichia coli Proteins ; Saccharomyces cerevisiae Proteins ; DNA (9007-49-2) ; Adenosine Triphosphatases (EC 3.6.1.-) ; SGS1 protein, S cerevisiae (EC 3.6.1.-) ; UvrD protein, E coli (EC 3.6.1.-) ; DNA Helicases (EC 3.6.4.-) ; RecQ Helicases (EC 3.6.4.12)
Language	English
Publishing date	2005-08-04
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M503325200
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Article: Saccharomyces cerevisiae Srs2 DNA helicase selectively blocks expansions of trinucleotide repeats.

Bhattacharyya, Saumitri / Lahue, Robert S

Molecular and cellular biology

2004 Volume 24, Issue 17, Page(s) 7324–7330

Abstract: Trinucleotide repeats (TNRs) undergo frequent mutations in families afflicted with certain neurodegenerative disorders and in model organisms. TNR instability is modulated both by the repeat tract itself and by cellular proteins. Here we identified the ... ...

Abstract	Trinucleotide repeats (TNRs) undergo frequent mutations in families afflicted with certain neurodegenerative disorders and in model organisms. TNR instability is modulated both by the repeat tract itself and by cellular proteins. Here we identified the Saccharomyces cerevisiae DNA helicase Srs2 as a potent and selective inhibitor of expansions. srs2 mutants had up to 40-fold increased expansion rates of CTG, CAG, and CGG repeats. The expansion phenotype was specific, as mutation rates at dinucleotide repeats, at unique sequences, or for TNR contractions in srs2 mutants were not altered. Srs2 is known to suppress inappropriate genetic recombination; however, the TNR expansion phenotype of srs2 mutants was largely independent of RAD51 and RAD52. Instead, Srs2 mainly functioned with DNA polymerase delta to block expansions. The helicase activity of Srs2 was important, because a point mutant lacking ATPase function was defective in blocking expansions. Purified Srs2 was substantially better than bacterial UvrD helicase at in vitro unwinding of a DNA substrate that mimicked a TNR hairpin. Disruption of the related helicase gene SGS1 did not lead to excess expansions, nor did wild-type SGS1 suppress the expansion phenotype of an srs2 strain. We conclude that Srs2 selectively blocks triplet repeat expansions through its helicase activity and primarily in conjunction with polymerase delta.
MeSH term(s)	DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Polymerase III/metabolism ; Genomic Instability ; Mutation ; Nucleic Acid Conformation ; Phenotype ; Recombination, Genetic ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Trinucleotide Repeat Expansion ; Trinucleotide Repeats
Chemical Substances	Saccharomyces cerevisiae Proteins ; SRS2 protein, S cerevisiae (125481-05-2) ; DNA Polymerase III (EC 2.7.7.-) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2004-09
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.24.17.7324-7330.2004
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Article: Rev1 enhances CAG.CTG repeat stability in Saccharomyces cerevisiae.

Collins, Natasha S / Bhattacharyya, Saumitri / Lahue, Robert S

DNA repair

2007 Volume 6, Issue 1, Page(s) 38–44

Abstract: Trinucleotide repeats (TNRs) frequently expand in certain human genetic diseases, often with devastating pathological consequences. TNR expansions require the addition of new DNA; accordingly, molecular models suggest aberrant DNA replication or error- ... ...

Abstract	Trinucleotide repeats (TNRs) frequently expand in certain human genetic diseases, often with devastating pathological consequences. TNR expansions require the addition of new DNA; accordingly, molecular models suggest aberrant DNA replication or error-prone repair synthesis as the sources of most instability. Some proteins are currently known that either promote or inhibit TNR mutability. To identify additional proteins that help protect cells against TNR instability, yeast mutants were isolated with higher than normal rates of CAG.CTG tract expansions. Surprisingly, a rev1 mutant was isolated. In contrast to its canonical function in supporting mutagenesis, we found that Rev1 reduces rates of CAG.CTG repeat expansions and contractions, as judged by the behavior of the rev1 mutant. The rev1 mutator phenotype was specific for TNRs with hairpin forming capacity. Mutations in REV3 or REV7, encoding the subunits of DNA polymerase zeta (pol zeta), did not affect expansion rates in REV1 or rev1 strains. A rev1 point mutant lacking dCMP transferase activity was normal for TNR instability, whereas the rev1-1 allele that interferes with BRCT domain function was as defective as a rev1 null mutant. In summary, these results indicate that yeast Rev1 reduces mutability of CAG.CTG tracts in a manner dependent on BRCT domain function but independent of dCMP transferase activity and of pol zeta.
MeSH term(s)	DNA Repair ; DNA Replication ; DNA, Fungal/genetics ; DNA, Fungal/metabolism ; DNA-Directed DNA Polymerase/genetics ; DNA-Directed DNA Polymerase/metabolism ; Mutation/genetics ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Trinucleotide Repeat Expansion
Chemical Substances	DNA, Fungal ; REV7 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; DNA polymerase zeta (EC 2.7.7.-) ; Nucleotidyltransferases (EC 2.7.7.-) ; REV1 protein, S cerevisiae (EC 2.7.7.-) ; DNA-Directed DNA Polymerase (EC 2.7.7.7) ; REV3 protein, S cerevisiae (EC 2.7.7.7)
Language	English
Publishing date	2007-01-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2006.08.002
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Article: Genetic assays for triplet repeat instability in yeast.

Dixon, Michael J / Bhattacharyya, Saumitri / Lahue, Robert S

Methods in molecular biology (Clifton, N.J.)

2004 Volume 277, Page(s) 29–45

Abstract: The unusual genetic features of trinucleotide repeat (TNR) diseases have stimulated a substantial body of research into the underlying molecular mechanisms of repeat instability. As one useful tool to study TNR instability, selectable genetic assays for ... ...

Abstract	The unusual genetic features of trinucleotide repeat (TNR) diseases have stimulated a substantial body of research into the underlying molecular mechanisms of repeat instability. As one useful tool to study TNR instability, selectable genetic assays for expansions and contractions were developed in the yeast Saccharomyces cerevisiae. These assays are sensitive, quantitative, easy to manipulate, and reproducible. Once colonies are identified through genetic selection, follow-up experiments with PCR help detail the precise molecular changes that occurred at the TNR tract. This chapter describes these yeast assays and provides useful technical insights into creating and testing triplet repeat instability in a classic model system.
MeSH term(s)	Animals ; Base Sequence ; Blotting, Southern ; Cattle ; DNA/genetics ; DNA Primers ; Polymerase Chain Reaction ; Saccharomyces cerevisiae/genetics ; Trinucleotide Repeats/genetics
Chemical Substances	DNA Primers ; DNA (9007-49-2)
Language	English
Publishing date	2004
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1385/1-59259-804-8:029
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Article ; Online: Chromosome breakage is regulated by the interaction of the BLM helicase and topoisomerase IIalpha.

Russell, Beatriz / Bhattacharyya, Saumitri / Keirsey, Jeremy / Sandy, April / Grierson, Patrick / Perchiniak, Erin / Kavecansky, Juraj / Acharya, Samir / Groden, Joanna

Cancer research

2011 Volume 71, Issue 2, Page(s) 561–571

Abstract: Cells deficient in the recQ-like helicase BLM are characterized by chromosome changes that suggest the disruption of normal mechanisms needed to resolve recombination intermediates and to maintain chromosome stability. Human BLM and topoisomerase IIα ... ...

Abstract	Cells deficient in the recQ-like helicase BLM are characterized by chromosome changes that suggest the disruption of normal mechanisms needed to resolve recombination intermediates and to maintain chromosome stability. Human BLM and topoisomerase IIα interact directly via amino acids 489-587 of BLM and colocalize predominantly in late G2 and M phases of the cell cycle. Deletion of this region does not affect the inherent in vitro helicase activity of BLM but inhibits the topoisomerase IIα-dependent enhancement of its activity, based on the analysis of specific DNA substrates that represent some recombination intermediates. Deletion of the interaction domain from BLM fails to correct the elevated chromosome breakage of transfected BLM-deficient cells. Our results demonstrate that the BLM-topoisomerase IIα interaction is important for preventing chromosome breakage and elucidate a DNA repair mechanism that is critical to maintain chromosome stability in cells and to prevent tumor formation.
MeSH term(s)	Antigens, Neoplasm/genetics ; Antigens, Neoplasm/metabolism ; Cell Cycle/physiology ; Cell Division/physiology ; Cell Line, Tumor ; Chromosome Breakage ; DNA Topoisomerases, Type II/genetics ; DNA Topoisomerases, Type II/metabolism ; DNA, Neoplasm/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; G2 Phase/physiology ; HCT116 Cells ; HeLa Cells ; Humans ; RecQ Helicases/genetics ; RecQ Helicases/metabolism ; Transfection
Chemical Substances	Antigens, Neoplasm ; DNA, Neoplasm ; DNA-Binding Proteins ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12) ; DNA Topoisomerases, Type II (EC 5.99.1.3)
Language	English
Publishing date	2011-01-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-10-1727
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Article ; Online: BLM helicase facilitates RNA polymerase I-mediated ribosomal RNA transcription.

Grierson, Patrick M / Lillard, Kate / Behbehani, Gregory K / Combs, Kelly A / Bhattacharyya, Saumitri / Acharya, Samir / Groden, Joanna

Human molecular genetics

2011 Volume 21, Issue 5, Page(s) 1172–1183

Abstract: Bloom's syndrome (BS) is an autosomal recessive disorder that is invariably characterized by severe growth retardation and cancer predisposition. The Bloom's syndrome helicase (BLM), mutations of which lead to BS, localizes to promyelocytic leukemia ... ...

Abstract	Bloom's syndrome (BS) is an autosomal recessive disorder that is invariably characterized by severe growth retardation and cancer predisposition. The Bloom's syndrome helicase (BLM), mutations of which lead to BS, localizes to promyelocytic leukemia protein bodies and to the nucleolus of the cell, the site of RNA polymerase I-mediated ribosomal RNA (rRNA) transcription. rRNA transcription is fundamental for ribosome biogenesis and therefore protein synthesis, cellular growth and proliferation; its inhibition limits cellular growth and proliferation as well as bodily growth. We report that nucleolar BLM facilitates RNA polymerase I-mediated rRNA transcription. Immunofluorescence studies demonstrate the dependance of BLM nucleolar localization upon ongoing RNA polymerase I-mediated rRNA transcription. In vivo protein co-immunoprecipitation demonstrates that BLM interacts with RPA194, a subunit of RNA polymerase I. (3)H-uridine pulse-chase assays demonstrate that BLM expression is required for efficient rRNA transcription. In vitro helicase assays demonstrate that BLM unwinds GC-rich rDNA-like substrates that form in the nucleolus and normally inhibit progression of the RNA polymerase I transcription complex. These studies suggest that nucleolar BLM modulates rDNA structures in association with RNA polymerase I to facilitate RNA polymerase I-mediated rRNA transcription. Given the intricate relationship between rDNA metabolism and growth, our data may help in understanding the etiology of proportional dwarfism in BS.
MeSH term(s)	Cell Line ; Cell Line, Tumor ; Cell Nucleolus/metabolism ; Cell Nucleus/metabolism ; DNA/chemistry ; DNA/metabolism ; DNA, Ribosomal/chemistry ; DNA, Ribosomal/metabolism ; Dactinomycin/pharmacology ; Humans ; Nucleic Acid Conformation ; Protein Binding ; Protein Subunits/metabolism ; RNA Polymerase I/antagonists & inhibitors ; RNA Polymerase I/metabolism ; RNA, Ribosomal/genetics ; RecQ Helicases/genetics ; RecQ Helicases/metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription, Genetic
Chemical Substances	DNA, Ribosomal ; Protein Subunits ; RNA, Ribosomal ; Recombinant Fusion Proteins ; Dactinomycin (1CC1JFE158) ; DNA (9007-49-2) ; RNA Polymerase I (EC 2.7.7.6) ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12)
Language	English
Publishing date	2011-11-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddr545
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Article: Telomerase-associated Protein 1, HSP90, and Topoisomerase IIα Associate Directly with the BLM Helicase in Immortalized Cells Using ALT and Modulate Its Helicase Activity Using Telomeric DNA Substrates

Bhattacharyya, Saumitri / Keirsey, Jeremy / Russell, Beatriz / Kavecansky, Juraj / Lillard-Wetherell, Kate / Tahmaseb, Kambiz / Turchi, John J / Groden, Joanna

Journal of biological chemistry. 2009 May 29, v. 284, no. 22

2009

Abstract: The BLM helicase associates with the telomere structural proteins TRF1 and TRF2 in immortalized cells using the alternative lengthening of telomere (ALT) pathways. This work focuses on identifying protein partners of BLM in cells using ALT. Mass ... ...

Abstract	The BLM helicase associates with the telomere structural proteins TRF1 and TRF2 in immortalized cells using the alternative lengthening of telomere (ALT) pathways. This work focuses on identifying protein partners of BLM in cells using ALT. Mass spectrometry and immunoprecipitation techniques have identified three proteins that bind directly to BLM and TRF2 in ALT cells: telomerase-associated protein 1 (TEP1), heat shock protein 90 (HSP90), and topoisomerase IIα (TOPOIIα). BLM predominantly co-localizes with these proteins in foci actively synthesizing DNA during late S and G₂/M phases of the cell cycle when ALT is thought to occur. Immunoprecipitation studies also indicate that only HSP90 and TOPOIIα are components of a specific complex containing BLM, TRF1, and TRF2 but that this complex does not include TEP1. TEP1, TOPOIIα, and HSP90 interact directly with BLM in vitro and modulate its helicase activity on telomere-like DNA substrates but not on non-telomeric substrates. Initial studies suggest that knockdown of BLM in ALT cells reduces average telomere length but does not do so in cells using telomerase.
Language	English
Dates of publication	2009-0529
Size	p. 14966-14977.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Telomerase-associated protein 1, HSP90, and topoisomerase IIalpha associate directly with the BLM helicase in immortalized cells using ALT and modulate its helicase activity using telomeric DNA substrates.

Bhattacharyya, Saumitri / Keirsey, Jeremy / Russell, Beatriz / Kavecansky, Juraj / Lillard-Wetherell, Kate / Tahmaseb, Kambiz / Turchi, John J / Groden, Joanna

The Journal of biological chemistry

2009 Volume 284, Issue 22, Page(s) 14966–14977

Abstract	The BLM helicase associates with the telomere structural proteins TRF1 and TRF2 in immortalized cells using the alternative lengthening of telomere (ALT) pathways. This work focuses on identifying protein partners of BLM in cells using ALT. Mass spectrometry and immunoprecipitation techniques have identified three proteins that bind directly to BLM and TRF2 in ALT cells: telomerase-associated protein 1 (TEP1), heat shock protein 90 (HSP90), and topoisomerase IIalpha (TOPOIIalpha). BLM predominantly co-localizes with these proteins in foci actively synthesizing DNA during late S and G(2)/M phases of the cell cycle when ALT is thought to occur. Immunoprecipitation studies also indicate that only HSP90 and TOPOIIalpha are components of a specific complex containing BLM, TRF1, and TRF2 but that this complex does not include TEP1. TEP1, TOPOIIalpha, and HSP90 interact directly with BLM in vitro and modulate its helicase activity on telomere-like DNA substrates but not on non-telomeric substrates. Initial studies suggest that knockdown of BLM in ALT cells reduces average telomere length but does not do so in cells using telomerase.
MeSH term(s)	Antigens, Neoplasm/metabolism ; Blotting, Western ; Carrier Proteins/metabolism ; Cell Line, Transformed ; Cell Nucleus Structures/metabolism ; DNA/biosynthesis ; DNA/metabolism ; DNA Topoisomerases, Type II/metabolism ; DNA-Binding Proteins/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Mass Spectrometry ; Protein Transport ; RNA-Binding Proteins ; RecQ Helicases/chemistry ; RecQ Helicases/metabolism ; Telomere/metabolism ; Telomeric Repeat Binding Protein 2/chemistry
Chemical Substances	Antigens, Neoplasm ; Carrier Proteins ; DNA-Binding Proteins ; HSP90 Heat-Shock Proteins ; RNA-Binding Proteins ; TEP1 protein, human ; TERF2 protein, human ; Telomeric Repeat Binding Protein 2 ; DNA (9007-49-2) ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12) ; DNA Topoisomerases, Type II (EC 5.99.1.3)
Language	English
Publishing date	2009-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M900195200
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