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Biochemistry & Molecular Biology

R76 in transmembrane domain 3 of the aspartate:alanine transporter AspT is involved in substrate transport

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Pages 744-747 | Received 24 Sep 2015, Accepted 11 Nov 2015, Published online: 05 Feb 2016

References

  • Nakamura J, Hirano S, Ito H, et al. Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce L-glutamic acid production. Appl. Environ. Microbiol. 2007;73:4491–4498.10.1128/AEM.02446-06
  • Enquist-Newman M, Faust AM, Bravo DD, et al. Efficient ethanol production from brown macroalgae sugars by a synthetic yeast platform. Nature. 2014;505:239–243.
  • Yamashita C, Hashimoto K, Kumagai K, et al. L-Glutamate secretion by the N-terminal domain of the corynebacterium glutamicum NCgl1221 mechanosensitive channel. Biosci. Biotechnol. Biochem. 2013;77:1008–1013.10.1271/bbb.120988
  • Abe K, Hayashi H, Maloney PC. Exchange of aspartate and alanine: mechanism for development of a proton-motive force in bacteria. J. Biol. Chem. 1996;271:3079–3084.10.1074/jbc.271.6.3079
  • Abe K, Ohnishi F, Yagi K, et al. Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction. J. Bacteriol. 2002;184:2906–2913.10.1128/JB.184.11.2906-2913.2002
  • Saier MH Jr, Tran CV, Barabote RD. TCDB: the transporter classification database for membrane transport protein analyses and information. Nucleic Acids Res. 2006;34:D181–D186.10.1093/nar/gkj001
  • Saier MH Jr, Yen MR, Noto K, et al. The transporter classification database: recent advances. Nucleic Acids Res. 2009;37:D274–D278.10.1093/nar/gkn862
  • Nanatani K, Maloney PC, Abe K. Structural and functional importance of transmembrane domain 3 (TM3) in the aspartate:alanine antiporter AspT: topology and function of the residues of TM3 and oligomerization of AspT. J. Bacteriol. 2009;191:2122–2132.10.1128/JB.00830-08
  • Sasahara A, Nanatani K, Enomoto M, et al. Substrate specificity of the aspartate:alanine antiporter (AspT) of Tetragenococcus halophilus in reconstituted liposomes. J. Biol. Chem. 2011;286:29044–29052.10.1074/jbc.M111.260224
  • Russ WP, Engelman DM. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 2000;296:911–919.10.1006/jmbi.1999.3489
  • Fukushima H, Mizutani M, Imamura K, et al. Development of a novel preparation method of recombinant proteoliposomes using baculovirus gene expression systems. J. Biochem. 2008;144:763–770.10.1093/jb/mvn125
  • Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 2012;9:671–675.10.1038/nmeth.2089
  • Fukui K, Koseki C, Yamamoto Y, et al. Identification of succinate exporter in Corynebacterium glutamicum and its physiological roles under anaerobic conditions. J. Biotechnol. 2011;154:25–34.10.1016/j.jbiotec.2011.03.010
  • Nanatani K, Fujiki T, Kanou K, et al. Topology of AspT, the aspartate:alanine antiporter of Tetragenococcus halophilus, determined by site-directed fluorescence labeling. J. Bacteriol. 2007;189:7089–7097.10.1128/JB.00088-07
  • Overton MC, Chinault SL, Blumer KJ. Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor. J. Biol. Chem. 2003;278:49369–49377.10.1074/jbc.M308654200
  • Kohlway A, Pirakitikulr N, Barrera FN, et al. Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain. J. Virol. 2014;88:628–642.10.1128/JVI.02052-13

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