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[DNA识别蛋白超结构α螺旋-转角-α螺旋在组蛋白中的预测]

[Prediction in histones of the DNA-recognizing protein superstructure alpha helix-turn-alpha helix].

作者信息

Shestopalov B V

出版信息

Mol Biol (Mosk). 1988 Mar-Apr;22(2):331-7.

PMID:3393145
Abstract

The localization of DNA-recognizing supersecondary structure alpha-helix--turn--alpha-helix in 85 amino acid sequences of histones is predicted. According to the prediction method based on the necessary requirements of amino acid coding this structure may be localized in the following segments of amino acid sequences of calf thymus histones: H1--90--112, H2A--54--76, H2B--50--72 and 102--124, H3--15--37 and 73--95, H4--5--27 or 6--28 and 32--54 or 42--64. According to the known experimental data on the secondary structure of histones only the following localizations are possible: H1--90--112, H2A--54--76, H2B--50--72, H3--73--95, H4--42--64. Using the known experimental data on DNA-histone interactions it is possible to suggest that these localizations of structures alpha-helix--turn--alpha-helix possible in histones H2A, H2B and H4 allows them to participate in close or structurally essential interactions of histones with DNA. The role of the predicted structure in nucleosome formation and in the autoregulation of histone biosynthesis is discussed.

摘要

预测了DNA识别超二级结构α-螺旋-转角-α-螺旋在85个组蛋白氨基酸序列中的定位。根据基于氨基酸编码必要条件的预测方法,该结构可能定位于小牛胸腺组蛋白氨基酸序列的以下片段:H1-90-112、H2A-54-76、H2B-50-72和102-124、H3-15-37和73-95、H4-5-27或6-28以及32-54或42-64。根据关于组蛋白二级结构的已知实验数据,仅以下定位是可能的:H1-90-112、H2A-54-76、H2B-50-72、H3-73-95、H4-42-64。利用关于DNA-组蛋白相互作用的已知实验数据,可以推测组蛋白H2A、H2B和H4中可能存在的这些α-螺旋-转角-α-螺旋结构定位使它们能够参与组蛋白与DNA的紧密或结构上必需的相互作用。讨论了预测结构在核小体形成和组蛋白生物合成的自动调节中的作用。

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