Alu-family repeat binding protein from HeLa cells which interacts with regulatory region of SV40 virus genome.

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Alu-family repeat binding protein from HeLa cells which interacts with regulatory region of SV40 virus genome. / Perelygina, LM; Tomilin, NV; Podgornaya, OI.

в: Molecular Biology Reports, Том 12, № 2, 1987, стр. 111-116.

Результаты исследований: Научные публикации в периодических изданиях › статья

BibTeX

@article{70661989a1a34f058e20965c79dbb45d,

title = "Alu-family repeat binding protein from HeLa cells which interacts with regulatory region of SV40 virus genome.",

abstract = "Using a gel retardation assay the protein which binds selectively to the Alu-family repeat (AFR) has been identified and partially purified from HeLa cell nuclear extract. The protein (AFR-binding protein, ABP) forms multiple discrete complexes with AFR even in the presence of 200 to 2000-fold excess of non-specific (E. coli) DNA. The most stable complex has a relative mobility in 4% polyacrylamide gel (as compared to the free Alu-fragment) of 0.54. Heterogeneity of protein-DNA bands seen in the polyacrylamide gel suggests that ABP is able to form multimeric complexes with AFR. Competition experiments show that ABP does not interact with the RNA polymerase III promoter and with the TGGCA-sequence, but a high affinity binding site for ABP was found within a 660 bp restriction fragment containing the SV40 virus promoter and replication origin.",

keywords = "DNA binding protein human cells",

author = "LM Perelygina and NV Tomilin and OI. Podgornaya",

year = "1987",

doi = "10.1007/BF00368878",

language = "не определен",

volume = "12",

pages = "111--116",

journal = "Molecular Biology Reports",

issn = "0301-4851",

publisher = "Springer Nature",

number = "2",

}

RIS

TY - JOUR

T1 - Alu-family repeat binding protein from HeLa cells which interacts with regulatory region of SV40 virus genome.

AU - Perelygina, LM

AU - Tomilin, NV

AU - Podgornaya, OI.

PY - 1987

Y1 - 1987

N2 - Using a gel retardation assay the protein which binds selectively to the Alu-family repeat (AFR) has been identified and partially purified from HeLa cell nuclear extract. The protein (AFR-binding protein, ABP) forms multiple discrete complexes with AFR even in the presence of 200 to 2000-fold excess of non-specific (E. coli) DNA. The most stable complex has a relative mobility in 4% polyacrylamide gel (as compared to the free Alu-fragment) of 0.54. Heterogeneity of protein-DNA bands seen in the polyacrylamide gel suggests that ABP is able to form multimeric complexes with AFR. Competition experiments show that ABP does not interact with the RNA polymerase III promoter and with the TGGCA-sequence, but a high affinity binding site for ABP was found within a 660 bp restriction fragment containing the SV40 virus promoter and replication origin.

AB - Using a gel retardation assay the protein which binds selectively to the Alu-family repeat (AFR) has been identified and partially purified from HeLa cell nuclear extract. The protein (AFR-binding protein, ABP) forms multiple discrete complexes with AFR even in the presence of 200 to 2000-fold excess of non-specific (E. coli) DNA. The most stable complex has a relative mobility in 4% polyacrylamide gel (as compared to the free Alu-fragment) of 0.54. Heterogeneity of protein-DNA bands seen in the polyacrylamide gel suggests that ABP is able to form multimeric complexes with AFR. Competition experiments show that ABP does not interact with the RNA polymerase III promoter and with the TGGCA-sequence, but a high affinity binding site for ABP was found within a 660 bp restriction fragment containing the SV40 virus promoter and replication origin.

KW - DNA binding protein human cells

U2 - 10.1007/BF00368878

DO - 10.1007/BF00368878

M3 - статья

VL - 12

SP - 111

EP - 116

JO - Molecular Biology Reports

JF - Molecular Biology Reports

SN - 0301-4851

IS - 2

ER -

ID: 5444310