JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.00265-08v1
190/13/4416    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Google Scholar
Right arrow Articles by Higgs, P. I.
Right arrow Articles by Zusman, D. R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Higgs, P. I.
Right arrow Articles by Zusman, D. R.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2008, p. 4416-4426, Vol. 190, No. 13
0021-9193/08/$08.00+0     doi:10.1128/JB.00265-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

EspA, an Orphan Hybrid Histidine Protein Kinase, Regulates the Timing of Expression of Key Developmental Proteins of Myxococcus xanthus{triangledown}

Penelope I. Higgs,1* Sakthimala Jagadeesan,1 Petra Mann,1 and David R. Zusman2

Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg D35043, Germany,1 Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-32042

Received 21 February 2008/ Accepted 26 March 2008

Myxococcus xanthus undergoes a complex starvation-induced developmental program that results in cells forming multicellular fruiting bodies by aggregating into mounds and then differentiating into spores. This developmental program requires at least 72 h and is mediated by a temporal cascade of gene regulators in response to intra- and extracellular signals. espA mutants, encoding an orphan hybrid histidine kinase, alter the timing of this developmental program, greatly accelerating developmental progression. Here, we characterized EspA and demonstrated that it autophosphorylates in vitro on the conserved histidine residue and then transfers the phosphoryl group to the conserved aspartate residue in the associated receiver domain. The conserved histidine and aspartate residues were both required for EspA function in vivo. Analysis of developmental gene expression and protein accumulation in espA mutants indicated that the expression of the A-signal-dependent spi gene was not affected but that the MrpC transcriptional regulator accumulated earlier, resulting in earlier expression of its target, the FruA transcriptional regulator. Early expression of FruA correlated with acceleration of both the aggregation and sporulation branches of the developmental program, as monitored by early methylation of the FrzCD chemosensory receptor and early expression of the sporulation-specific dev and Mxan_3227 ({Omega}7536) genes. These results show that EspA plays a key role in the timing of expression of genes necessary for progression of cells through the developmental program.


* Corresponding author. Mailing address: Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse 1, 35043 Marburg, Germany. Phone: (49) 6421 178301. Fax: (49) 6421 178309. E-mail: higgs{at}mpi-marburg.mpg.de

{triangledown} Published ahead of print on 4 April 2008.


Journal of Bacteriology, July 2008, p. 4416-4426, Vol. 190, No. 13
0021-9193/08/$08.00+0     doi:10.1128/JB.00265-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2008 by the American Society for Microbiology. All rights reserved.