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SV40 T抗原的起始结合形式中只有一种具有解旋酶活性。

Only one of the origin binding forms of SV40 T antigen has helicase activity.

作者信息

Deb S P, Partin K

机构信息

Department of Microbiology, State University of New York, Stony Brook 11794.

出版信息

Biochem Biophys Res Commun. 1988 May 31;153(1):249-55. doi: 10.1016/s0006-291x(88)81215-4.

Abstract

SV40 T antigen exists in monomeric and multimeric forms. We have separated the individual components by glycerol gradient centrifugation. Helicase activity is found to be associated with monomeric forms only. Dimers and other multimeric forms have no discernable helicase activity. However, results obtained from DNA binding experiments carried out with separated forms of T antigen indicate that both monomers and dimers bind to region I and region II of SV40 origin of replication. Possibly monomeric T antigen unwinds DNA at the replication fork while both monomeric and dimeric forms are utilized for positioning of T antigen at the origin of replication.

摘要

SV40 T抗原以单体和多聚体形式存在。我们通过甘油梯度离心分离了各个组分。发现解旋酶活性仅与单体形式相关。二聚体和其他多聚体形式没有可识别的解旋酶活性。然而,用分离形式的T抗原进行的DNA结合实验结果表明,单体和二聚体都与SV40复制起点的区域I和区域II结合。可能单体T抗原在复制叉处解开DNA,而单体和二聚体形式都用于将T抗原定位在复制起点。

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