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000032545 0247_ $$2DOI$$a10.1016/j.jmb.2003.08.034
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000032545 084__ $$2WoS$$aBiochemistry & Molecular Biology
000032545 1001_ $$0P:(DE-HGF)0$$aMenezes, R. A.$$b0
000032545 245__ $$aSites for Interaction between Gal80p and Gal1p in Kluyveromyces latis: Structural Model of Galactokinase based on Homology to the GHMP Protein Family
000032545 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2003
000032545 300__ $$a479 - 492
000032545 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000032545 440_0 $$03552$$aJournal of Molecular Biology$$v333$$x0022-2836$$y3
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000032545 520__ $$aThe induction of transcription of the galactose genes in yeast involves the galactose-dependent binding of ScGal3p (in Saccharomyces cerevisiae) or KlGal1p (in Kluyveromyces lactis) to Gal80p. This binding abrogates Gal80's inhibitory effect on the activation domain of Gal4p, which can then activate transcription. Here, we describe the isolation and characterization of new interaction mutants of K. lactis GAL1 and GAL80 using a two-hybrid screen. We present the first structural model for Gal1p to be based on the published crystal structures of other proteins belonging to the GHMP (galactokinase, homoserine kinase, mevalonate kinase and phosphomevalonate kinase) kinase family and our own X-ray diffraction data of Gal1p crystals at 3 Angstrom resolution.The locations of the various mutations in the modelled Gal1p structure identify domains involved in the interaction with Gal80p and provide a structural explanation for the phenotype of constitutive GAL1 mutations. (C) 2003 Elsevier Ltd. All rights reserved.
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000032545 65320 $$2Author$$aKluyveromyces lactis
000032545 65320 $$2Author$$aGal1p-Gal80p interaction
000032545 65320 $$2Author$$aprotein interaction
000032545 65320 $$2Author$$aGal1p protein structure
000032545 65320 $$2Author$$agalactose induction
000032545 7001_ $$0P:(DE-HGF)0$$aAmuel, C.$$b1
000032545 7001_ $$0P:(DE-HGF)0$$aEngels, R.$$b2
000032545 7001_ $$0P:(DE-HGF)0$$aGengenbacher, U.$$b3
000032545 7001_ $$0P:(DE-Juel1)VDB886$$aLabahn, J.$$b4$$uFZJ
000032545 7001_ $$0P:(DE-HGF)0$$aHollenberg, E. M.$$b5
000032545 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2003.08.034$$gVol. 333, p. 479 - 492$$p479 - 492$$q333<479 - 492$$tJournal of molecular biology$$v333$$x0022-2836$$y2003
000032545 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2003.08.034
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000032545 9141_ $$y2003
000032545 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000032545 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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