Mannermaa R M, Oikarinen J
Collagen Research Unit, University of Oulu, Finland.
Biochem Biophys Res Commun. 1992 Jan 15;182(1):309-17. doi: 10.1016/s0006-291x(05)80146-9.
We present here further evidence supporting that histone H1 contains a nucleotide binding site interacting e.g. with ADP, ATP, GDP and GTP. The finding is in accordance with the previous observation that nucleotides modulate recognition of DNA by H1. Most interestingly, H1 appears to be capable of hydrolyzing NTPs and incorporating phosphate to exogenous proteins. The mode of nucleotide action on H1 may be considered highly analogous to that of GTPases. Nuclear receptors may thus act through mechanisms similar to those for receptors on the plasma membrane.
我们在此展示了进一步的证据，支持组蛋白H1含有一个核苷酸结合位点，该位点可与例如ADP、ATP、GDP和GTP相互作用。这一发现与之前的观察结果一致，即核苷酸可调节H1对DNA的识别。最有趣的是，H1似乎能够水解NTP并将磷酸基团掺入外源蛋白质中。核苷酸对H1的作用方式可能与GTP酶的作用方式高度相似。因此，核受体可能通过与质膜上受体类似的机制发挥作用。
