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  Structure and Function of the Universal Stress Protein TeaD and its Role in Regulating the Ectoine Transporter TeaABC of Halomonas elongata DSM 2581T

Schweikhard, E. S., Kuhlmann, S. I., Kunte, H.-J., Grammann, K., & Ziegler, C. M. (2010). Structure and Function of the Universal Stress Protein TeaD and its Role in Regulating the Ectoine Transporter TeaABC of Halomonas elongata DSM 2581T. Biochemistry, 49(10), 2194-2204. doi:10.1021/bi9017522.

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 Creators:
Schweikhard, Eva S.1, Author           
Kuhlmann, Sonja I.1, Author           
Kunte, Hans-Jörg, Author
Grammann, Katrin, Author
Ziegler, Christine M.1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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 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.

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Language(s): eng - English
 Dates: 2010-03
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 476387
DOI: 10.1021/bi9017522
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 49 (10) Sequence Number: - Start / End Page: 2194 - 2204 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103