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环磷酸腺苷（cAMP）和环磷酸鸟苷（cGMP）与大肠杆菌环磷酸腺苷受体蛋白CRP*598突变体结合的特性研究

Characterization of the binding of cAMP and cGMP to the CRP*598 mutant of the E. coli cAMP receptor protein.

作者信息

Ren Y L, Garges S, Adhya S, Krakow J S

机构信息

Department of Biological Sciences, Hunter College, CUNY, NY 10021.

出版信息

Nucleic Acids Res. 1990 Sep 11;18(17):5127-32. doi: 10.1093/nar/18.17.5127.

DOI:10.1093/nar/18.17.5127

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC332133/

Abstract

Wild type cAMP receptor protein (CRP) activates in vitro lac transcription only in the presence of cAMP. In contrast the mutant CRP598 (Arg-142 to His, Ala-144 to Thr) can activate lac transcription in the absence of cyclic nucleotide or at concentrations of cAMP below that required by CRP. To further characterize the properties of CRP598, the binding of cAMP and cGMP to CRP and CRP598 has been determined. The intrinsic binding constant (K) values obtained for cAMP binding are: CRP, 1.9 x 10(4) M-1; CRP598, 3.8 x 10(5) M-1. The K values obtained for cGMP binding are: CRP, 2.9 x 10(4) M-1; CRP598, 2.7 x 10(4) M-1. The results indicate that the affinity of CRP and CRP598 for cGMP is relatively unchanged while the affinity of CRP598 for cAMP is approximately twenty times greater than that shown by CRP. Binding of cAMP by CRP and cGMP by CRP or CRP598 exhibits slight negative cooperativity. The major difference seen is that CRP598 binds cAMP with strong positive cooperativity. The importance of the unsubstituted N6 position of the adenine moiety is also shown by the similar affinity of both forms of CRP for N6-butyryl cAMP. The cAMP binding properties evinced by CRP598 suggest that its intrinsically altered conformation may be related to that assumed by CRP in a CRP-DNA or a cAMP-CRP-DNA complex.

摘要

野生型环磷酸腺苷（cAMP）受体蛋白（CRP）仅在有cAMP存在时才能在体外激活乳糖操纵子转录。相比之下，突变型CRP598（第142位精氨酸突变为组氨酸，第144位丙氨酸突变为苏氨酸）在没有环核苷酸的情况下或在低于CRP所需浓度的cAMP存在时就能激活乳糖操纵子转录。为了进一步表征CRP598的特性，已测定了cAMP和cGMP与CRP及CRP598的结合情况。cAMP结合的内在结合常数（K）值如下：CRP为1.9×10⁴ M⁻¹；CRP598为3.8×10⁵ M⁻¹。cGMP结合的K值如下：CRP为2.9×10⁴ M⁻¹；CRP598为2.7×10⁴ M⁻¹。结果表明，CRP和CRP598对cGMP的亲和力相对不变，而CRP598对cAMP的亲和力约为CRP的20倍。CRP与cAMP的结合以及CRP或CRP598与cGMP的结合表现出轻微的负协同性。观察到的主要差异在于CRP598与cAMP结合时具有强烈的正协同性。两种形式的CRP对N⁶-丁酰基cAMP的相似亲和力也表明了腺嘌呤部分未被取代的N⁶位置的重要性。CRP598所表现出的cAMP结合特性表明，其内在改变的构象可能与CRP在CRP-DNA或cAMP-CRP-DNA复合物中所呈现的构象有关。