Structural and functional analysis of the cAMP binding domain from the regulatory subunit of Mucor rouxii protein kinase A
The cAMP binding domain of the regulatory subunit (R) of Mucor rouxii protein kinase A was cloned. The deduced amino acid sequence was highly homologous in sequence and in size to the corresponding region in fungal and higher eukaryotic regulatory subunits (47-54%), but particularly homologous (62%)...
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| Otros Autores: | , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Academic Press Inc.
2000
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 08888caa a22012137a 4500 | ||
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| 001 | PAPER-2254 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203138.0 | ||
| 008 | 190411s2000 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0034667984 | |
| 024 | 7 | |2 Molecular Sequence Numbers |a GENBANK: AF240461; DDBJ: AF240461; | |
| 024 | 7 | |2 cas |a amino acid, 65072-01-7; arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; cyclic AMP, 60-92-4; cyclic AMP dependent protein kinase; leucine, 61-90-5, 7005-03-0; lysine, 56-87-1, 6899-06-5, 70-54-2 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a ABBIA | ||
| 100 | 1 | |a Sorol, M.R. | |
| 245 | 1 | 0 | |a Structural and functional analysis of the cAMP binding domain from the regulatory subunit of Mucor rouxii protein kinase A |
| 260 | |b Academic Press Inc. |c 2000 | ||
| 270 | 1 | 0 | |m Rossi, S.; Departamento de Quimica Biologica, Fac. de Ciencias Exact. y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina; email: srossi@qb.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Su, Y., Dostmann, W.R.G., Herberg, F.W., Durick, K., Xuong, N., Ten Eyck, L.F., Taylor, S.S., Varughese, K.I., (1995) Science, 269, pp. 807-813 | ||
| 504 | |a Gibson, R.M., Ji-Buechler, Y., Taylor, S.S., (1997) J. Biol. Chem., 272, pp. 16343-16350 | ||
| 504 | |a Moreno, S., Passeron, S., (1980) Arch. Biochem. Biophys., 199, pp. 321-330 | ||
| 504 | |a Pastori, R., Moreno, S., Passeron, S., (1985) Mol. Cell. Biochem., 69, pp. 55-66 | ||
| 504 | |a Paveto, C., Passeron, S., Corbin, J.D., Moreno, S., (1989) Eur. J. Biochem., 179, pp. 429-434 | ||
| 504 | |a Rossi, S., Guthmann, M., Moreno, S., (1992) Cell. Signal., 4, pp. 443-451 | ||
| 504 | |a Pastori, R., Kerner, N., Moreno, S., Passeron, S., (1981) Biochem. Biophys. Res. Commun., 101, pp. 663-671 | ||
| 504 | |a Guthmann, M., Pastori, R., Moreno, S., (1990) Cell. Signal., 2, pp. 395-402 | ||
| 504 | |a Hoffman, C.S., Winston, D., (1987) Gene, 57, pp. 267-272 | ||
| 504 | |a Ausubel, F.M., Brent, R., Kingston, R., Moore, D., Seidman, J.G., Smith, J.A., Struhl, K., (1993) Short Protocols in Molecular Biology, 2nd ed., , Greene Publishing Associates/Wiley, New York | ||
| 504 | |a Peitsch, M.C., (1995) Biotechnology, 13, pp. 658-660 | ||
| 504 | |a Peitsch, M.C., (1996) Biochem. Soc. Trans., 24, pp. 274-279 | ||
| 504 | |a Guex, N., Peitsch, M.C., (1977) Electrophoresis, 18, pp. 2714-2723 | ||
| 504 | |a Tanabe, Y., Nagahama, T., Saikawa, M., Sugiyama, J., (1999) Mycologia, 91, pp. 830-835 | ||
| 504 | |a Thon, M.R., Royse, D.J., (1999) Mycologia, 91, pp. 468-474 | ||
| 504 | |a Cho-Chung, Y.S., Clair, T., (1993) Pharmacol. Ther., 60, pp. 265-288 | ||
| 504 | |a Tasken, T., Skalhegg, B.S., Tasken, K.A., Solberg, R., Knutsen, H.K., Levy, F.O., Sandberg, M., Jahnsen, T., (1997) Adv. Second Messenger Phosphoprotein Res., 31, pp. 191-204 | ||
| 504 | |a Shabb, J.B., Corbin, J.D., (1992) J. Biol. Chem., 267, pp. 5723-5726 | ||
| 504 | |a Zhao, J., Hoye, E., Boylan, S., Walsh, D.A., Trewhella, J., (1998) J. Biol. Chem., 273, pp. 30448-30459 | ||
| 504 | |a Gibbs, C.S., Zoller, M.J., (1991) J. Biol. Chem., 266, pp. 8923-8931 | ||
| 504 | |a Gibbs, C.S., Knighton, D.R., Sowadski, J.M., Taylor, S.S., Zoller, M.J., (1992) J. Biol. Chem., 267, pp. 4806-4814 | ||
| 504 | |a Orellana, S.A., Amieux, P.S., Zhao, X., McKnight, G.S., (1993) J. Biol. Chem., 268, pp. 6843-6846 | ||
| 504 | |a Gibson, R.M., Buechler, Y.J., Taylor, S.S., (1997) Protein Sci., 6, pp. 1825-1834 | ||
| 504 | |a Huang, L.J., Taylor, S.S., (1998) J. Biol. Chem., 273, pp. 26739-26746 | ||
| 504 | |a Kuret, J., Johnson, K.E., Nicolette, C., Zoller, M.J., (1988) J. Biol. Chem., 263, pp. 9149-9154 | ||
| 504 | |a Woodford, T.A., Correll, L.A., McKnight, G.S., Corbin, J.D., (1989) J. Biol. Chem., 264, pp. 13321-13328 | ||
| 504 | |a Garbers, D.L., First, N.L., Lardy, H.A., (1973) J. Biol. Chem., 248, pp. 875-879 | ||
| 504 | |a Srivastava, A.K., Stellwagen, R.H., (1978) J. Biol. Chem., 253, pp. 1752-1755 | ||
| 504 | |a Takai, Y., Yamamura, H., Nishizuka, Y., (1974) J. Biol. Chem., 249, pp. 530-535 | ||
| 504 | |a Rannels, S.R., Corbin, J.D., (1979) J. Biol. Chem., 254, pp. 8605-8610 | ||
| 504 | |a Rannels, S.R., Corbin, J.D., (1980) J. Cycl. Nucleotide Res., 8, pp. 201-215 | ||
| 504 | |a Shabb, J.B., Poteet, C.E., Kapphahn, M.A., Muhonen, W.M., Baker, N.E., Corbin, J.D., (1995) Protein Sci., 4, pp. 2100-2106 | ||
| 520 | 3 | |a The cAMP binding domain of the regulatory subunit (R) of Mucor rouxii protein kinase A was cloned. The deduced amino acid sequence was highly homologous in sequence and in size to the corresponding region in fungal and higher eukaryotic regulatory subunits (47-54%), but particularly homologous (62%) to Blastocladiella emersonii, a fungus classified in a different phylum. Amino acids reported to be important for interaction with cAMP, for cooperativity between the two cAMP binding domains, in the general folding of the domain, and for interaction with the catalytic subunit were conserved in all the fungal sequences. Based on either sequence or functional behavior, the M. rouxii R subunit cannot be classified as being more similar to RI or RII of mammalian systems. The M. rouxii protein sequence was modeled using as template the coordinates of the crystallized bovine regulatory subunit type I(α). The quality of the model is good. The two backbones could be perfectly overlapped, except for two loop regions of high divergence. The α helix C of domain A, proposed to have a strong interaction with the catalytic subunit, contains a leucine replacing a basic residue (arginine or lysine) commonly found in RI or RII. The domains A and B of the M. rouxii regulatory subunit were overexpressed as fusion proteins with GST. GST domain B protein was inactive. GST domain A was active; the kinetic parameters of affinity toward cAMP analogs, site selectivity, and dissociation kinetics of bound cAMP were analogous to the properties of the domain in the whole regulatory subunit. (C) 2000 Academic Press. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: 1This work was supported by grants from the University of Buenos Aires, Agencia Nacional de Promoción Científ ica y Técnológica and Consejo Nacional de Investigaciones Científicas y Técnicas. M.R.S. had a doctoral fellowship and S.R. a postdoctoral short fellowship from FOMEC. | ||
| 593 | |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428, Buenos Aires, Argentina | ||
| 593 | |a Diabetes Research Institute, University of Miami, Miami, FL 33021, United States | ||
| 593 | |a International Center for Genetic Engineering and Biotechnology, Trieste, I-34012, Italy | ||
| 690 | 1 | 0 | |a CAMP BINDING |
| 690 | 1 | 0 | |a MUCOR ROUXII |
| 690 | 1 | 0 | |a PROTEIN SEQUENCE |
| 690 | 1 | 0 | |a AMINO ACID |
| 690 | 1 | 0 | |a ARGININE |
| 690 | 1 | 0 | |a CYCLIC AMP |
| 690 | 1 | 0 | |a CYCLIC AMP DEPENDENT PROTEIN KINASE |
| 690 | 1 | 0 | |a CYCLIC AMP DERIVATIVE |
| 690 | 1 | 0 | |a HYBRID PROTEIN |
| 690 | 1 | 0 | |a LEUCINE |
| 690 | 1 | 0 | |a LYSINE |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BINDING AFFINITY |
| 690 | 1 | 0 | |a CHEMICAL STRUCTURE |
| 690 | 1 | 0 | |a DISSOCIATION |
| 690 | 1 | 0 | |a ENZYME ACTIVE SITE |
| 690 | 1 | 0 | |a MOLECULAR MODEL |
| 690 | 1 | 0 | |a MUCOR |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a NUCLEOTIDE SEQUENCE |
| 690 | 1 | 0 | |a POLYMERASE CHAIN REACTION |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a SEQUENCE HOMOLOGY |
| 690 | 1 | 0 | |a AMYLOMYCES ROUXII |
| 690 | 1 | 0 | |a BLASTOCLADIELLA EMERSONII |
| 690 | 1 | 0 | |a BLASTOCLADIELLA EMERSONII |
| 690 | 1 | 0 | |a BOVINAE |
| 690 | 1 | 0 | |a EUKARYOTA |
| 690 | 1 | 0 | |a FUNGI |
| 690 | 1 | 0 | |a MAMMALIA |
| 690 | 1 | 0 | |a MUCOR |
| 690 | 1 | 0 | |a MUCOR ROUXII |
| 700 | 1 | |a Pastori, R.L. | |
| 700 | 1 | |a Muro, A. | |
| 700 | 1 | |a Moreno, S. | |
| 700 | 1 | |a Rossi, S. | |
| 773 | 0 | |d Academic Press Inc., 2000 |g v. 382 |h pp. 173-181 |k n. 2 |p Arch. Biochem. Biophys. |x 00039861 |w (AR-BaUEN)CENRE-1377 |t Archives of Biochemistry and Biophysics | |
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| 856 | 4 | 0 | |u https://doi.org/10.1006/abbi.2000.2018 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00039861_v382_n2_p173_Sorol |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v382_n2_p173_Sorol |y Registro en la Biblioteca Digital |
| 961 | |a paper_00039861_v382_n2_p173_Sorol |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 963 | |a VARI | ||
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