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J. Biol. Chem., Vol. 278, Issue 47, 46288-46292, November 21, 2003

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A Purple-blue Chromoprotein from Goniopora tenuidens Belongs to the DsRed Subfamily of GFP-like Proteins^*

Vladimir I. Martynov, Boris I. Maksimov¶, Natalya Y. Martynova, Alexey A. Pakhomov, Nadya G. Gurskaya, and Sergey A. Lukyanov

From the Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia and ^¶Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, 119121 Moscow, Russia

A number of recently cloned chromoproteins homologous to the green fluorescent protein show a substantial bathochromic shift in absorption spectra. Compared with red fluorescent protein from Discosoma sp. (DsRed), mutants of these so-called far-red proteins exhibit a clear red shift in emission spectra as well. Here we report that a far-red chromoprotein from Goniopora tenuidens (gtCP) contains a chromophore of the same chemical structure as DsRed. Denaturation kinetics of both DsRed and gtCP under acidic conditions indicates that the red form of the chromophore (absorption maximum at 436 nm) converts to the GFP-like form (384 nm) by a one-stage reaction. Upon neutralization, the 436-nm form of gtCP, but not the 384-nm form, renaturates instantly, implying that the former includes a chromophore in its intact state. gtCP represents a single-chain protein and, upon harsh denaturing conditions, shows three major bands in SDS/PAGE, two of which apparently result from hydrolysis of an acylimine C=N bond. Instead of having absorption maxima at 384 nm and 450 nm, which are characteristic for a GFP-like chromophore, fragmented gtCP shows a different spectrum, which presumably corresponds to a 2-keto derivative of imidazolidinone. Mass spectra of the chromophore-containing peptide from gtCP reveal an additional loss of 2 Da relative to the GFP-like chromophore. Tandem mass spectrometry of the chromopeptide shows that an additional bond is dehydrogenated in gtCP at the same position as in DsRed. Altogether, these data suggest that gtCP belongs to the same subfamily as DsRed (in the classification of GFP-like proteins based on the chromophore structure type).

Received for publication, June 26, 2003 , and in revised form, September 4, 2003.

^* This work was supported by the European Office of Aerospace Research and Development, Air Force Office of Scientific Research, Air Force Research Laboratory, under International Science and Technology Center Partner Project Agreement 2325, by Russian Foundation for Basic Research Grant 02–04-48054 (to V. I. M.), and by a Russian Academy of Sciences grant in the framework of program "Physicochemical Biology" (to N. G. G. and S. A. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, Miklukho-Maklaya 16/10, 117997 Moscow, Russia. Tel.: 7-095-336-5111; E-mail: vimart{at}ibch.ru.

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