The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain

Michel K-P, Schröder A-K, Zimmermann M, Brandt S, Pistorius EK, Frankenberg-Dinkel N, Staiger D (2009)
Archives of Microbiology 191(6): 553-559.

Download
OA
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ; ;
Abstract / Bemerkung
The cyanobacterium Synechocystis sp. PCC 6803 harbours 47 histidine kinases (Hiks). Among these are hybrid histidine kinases with one or two response regulator domains as well as numerous Hiks with several sensory domains. One example is the hybrid histidine kinase Slr1759 (Hik14) that has two PAS domains arranged in tandem linked to a predicted GAF domain. Here, we show that a Slr1759 derivative recombinantly expressed in Escherichia coli has a flavin cofactor. Using truncated Slr1759 variants, it is shown that the flavin associates with the first PAS domain. The cofactor reconstitutes the activity of d -amino acid oxidase apoprotein from pig kidney, indicating that the flavin derivative is FAD. Furthermore, the Slr1759 histidine kinase domain indeed undergoes autophosphorylation in vitro. The phosphorylated product of a recombinant Slr1759 derivative is sensitive to acids, pointing to a histidine residue as the phosphate-accepting group.
Erscheinungsjahr
Zeitschriftentitel
Archives of Microbiology
Band
191
Zeitschriftennummer
6
Seite
553-559
ISSN
eISSN
PUB-ID

Zitieren

Michel K-P, Schröder A-K, Zimmermann M, et al. The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain. Archives of Microbiology. 2009;191(6):553-559.
Michel, K. - P., Schröder, A. - K., Zimmermann, M., Brandt, S., Pistorius, E. K., Frankenberg-Dinkel, N., & Staiger, D. (2009). The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain. Archives of Microbiology, 191(6), 553-559. doi:10.1007/s00203-009-0483-x
Michel, K. - P., Schröder, A. - K., Zimmermann, M., Brandt, S., Pistorius, E. K., Frankenberg-Dinkel, N., and Staiger, D. (2009). The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain. Archives of Microbiology 191, 553-559.
Michel, K.-P., et al., 2009. The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain. Archives of Microbiology, 191(6), p 553-559.
K.-P. Michel, et al., “The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain”, Archives of Microbiology, vol. 191, 2009, pp. 553-559.
Michel, K.-P., Schröder, A.-K., Zimmermann, M., Brandt, S., Pistorius, E.K., Frankenberg-Dinkel, N., Staiger, D.: The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain. Archives of Microbiology. 191, 553-559 (2009).
Michel, Klaus-Peter, Schröder, Ann-Kristin, Zimmermann, Maike, Brandt, Sonja, Pistorius, Elfriede K., Frankenberg-Dinkel, Nicole, and Staiger, Dorothee. “The hybrid histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. PCC 6803 contains FAD at its PAS domain”. Archives of Microbiology 191.6 (2009): 553-559.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Copyright Statement:
This Item is protected by copyright and/or related rights. [...]
Volltext(e)
Access Level
OA Open Access
Zuletzt Hochgeladen
2011-11-30T00:33:37Z

31 References

Daten bereitgestellt von Europe PubMed Central.

PAS domains: internal sensors of oxygen, redox potential, and light.
Taylor BL, Zhulin IB., Microbiol. Mol. Biol. Rev. 63(2), 1999
PMID: 10357859
Histidine kinases and response regulator proteins in two-component signaling systems.
West AH, Stock AM., Trends Biochem. Sci. 26(6), 2001
PMID: 11406410
A two-component Mn2+-sensing system negatively regulates expression of the mntCAB operon in Synechocystis.
Yamaguchi K, Suzuki I, Yamamoto H, Lyukevich A, Bodrova I, Los DA, Piven I, Zinchenko V, Kanehisa M, Murata N., Plant Cell 14(11), 2002
PMID: 12417709

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 19424679
PubMed | Europe PMC

Suchen in

Google Scholar