Structure and function of the universal stress protein TeaD and its role in regulating the ectoine transporter TeaABC of Halomonas elongata DSM 2581(T)

Biochemistry
Eva S SchweikhardChristine Ziegler

Abstract

The halophilic bacterium Halomonas elongata takes up the compatible solute ectoine via the osmoregulated TRAP transporter TeaABC. A fourth orf (teaD) is located adjacent to the teaABC locus that encodes a putative universal stress protein (USP). By RT-PCR experiments we proved a cotranscription of teaD along with teaABC. Deletion of teaD resulted in an enhanced uptake for ectoine by the transporter TeaABC and hence a negative activity regulation of TeaABC by TeaD. A transcriptional regulation via DNA binding could be excluded. ATP binding to native TeaD was shown by HPLC, and the crystal structure of TeaD was solved in complex with ATP to a resolution of 1.9 A by molecular replacement. TeaD forms a dimer-dimer complex with one ATP molecule bound to each monomer, which has a Rossmann-like alpha/beta overall fold. Our results reveal an ATP-dependent oligomerization of TeaD, which might have a functional role in the regulatory mechanism of TeaD. USP-encoding orfs, which are located adjacent to genes encoding for TeaABC homologues, could be identified in several other organisms, and their physiological role in balancing the internal cellular ectoine pool is discussed.

References

Dec 1, 1976·Bacteriological Reviews·A D Brown
Oct 1, 1992·International Journal of Systematic Bacteriology·M J GauthierJ C Bertrand
Oct 5, 1990·Journal of Molecular Biology·S F AltschulD J Lipman
Jan 1, 1997·Nucleic Acids Research·L Holm, C Sander
Apr 1, 1997·Nature Structural Biology·K Diederichs, P A Karplus
Dec 23, 1998·Proceedings of the National Academy of Sciences of the United States of America·T I ZarembinskiS H Kim
Aug 31, 2000·Journal of Molecular Biology·C NotredameJ Heringa
Aug 29, 2001·FEMS Microbiology Reviews·D J Kelly, G H Thomas
Dec 12, 2001·Structure·M C Sousa, D B McKay
May 7, 2003·Current Opinion in Microbiology·Kristian KvintThomas Nyström
Aug 2, 2003·Research in Microbiology·Ronan O'Toole, Huw D Williams
Sep 1, 1994·Acta Crystallographica. Section D, Biological Crystallography·UNKNOWN Collaborative Computational Project, Number 4
May 1, 1997·Acta Crystallographica. Section D, Biological Crystallography·G N MurshudovE J Dodson
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·Serge X CohenAnastassis Perrakis
Apr 6, 2005·Acta Crystallographica. Section D, Biological Crystallography·Jay Painter, Ethan A Merritt
May 26, 2005·Protein Expression and Purification·F William Studier
Aug 15, 2006·Biochimica Et Biophysica Acta·Ravi D BaraboteMilton H Saier
Dec 14, 2006·Acta Crystallographica. Section D, Biological Crystallography·Airlie J McCoy
Apr 14, 2009·Journal of Molecular Biology·Justin LecherErhard Bremer

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Citations

Jan 19, 2013·Journal of Chemical Information and Modeling·Tuomo KalliokoskiAnna Vulpetti
Apr 16, 2011·Canadian Journal of Microbiology·Selim CeylanDilek Kazan
Jun 8, 2013·Evolutionary Applications·Karolina L TkaczukWladek Minor
Apr 9, 2020·Extremophiles : Life Under Extreme Conditions·Jasmina VandrichHans Jörg Kunte
Oct 6, 2016·International Journal of Environmental Research and Public Health·Priscilla MasambaAbidemi Paul Kappo
Jan 25, 2020·Nature Chemical Biology·Sarah ThorwallIan Wheeldon
May 15, 2021·The Journal of Biological Chemistry·Anirudha DuttaVijay Parashar

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