This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Park, D.
Right arrow Articles by Taghert, P. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Park, D.
Right arrow Articles by Taghert, P. H.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, January 2008, p. 410-421, Vol. 28, No. 1
0270-7306/08/$08.00+0     doi:10.1128/MCB.01104-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Drosophila Basic Helix-Loop-Helix Protein DIMMED Directly Activates PHM, a Gene Encoding a Neuropeptide-Amidating Enzyme{triangledown} ,{dagger}

Dongkook Park,1 Orie T. Shafer,1 Stacie P. Shepherd,1,2 Hyunsuk Suh,3 Jennifer S. Trigg,1 and Paul H. Taghert1*

Department of Anatomy and Neurobiology,1 Department of Pediatrics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, Missouri 63110,2 School of Biological Sciences, College of Natural Sciences, Seoul National University, 56-1 Shinlimdong Kwanakgu, Seoul 151-742, South Korea3

Received 21 June 2007/ Returned for modification 20 August 2007/ Accepted 22 October 2007

The basic helix-loop-helix (bHLH) protein DIMMED (DIMM) supports the differentiation of secretory properties in numerous peptidergic cells of Drosophila melanogaster. DIMM is coexpressed with diverse amidated neuropeptides and with the amidating enzyme peptidylglycine {alpha}-hydroxylating monooxygenase (PHM) in approximately 300 cells of the late embryo. Here we confirm that DIMM has transcription factor activity in transfected HEK 293 cells and that the PHM gene is a direct target. The mammalian DIMM orthologue MIST1 also transactivated the PHM gene. DIMM activity was dependent on the basic region of the protein and on the sequences of three E-box sites within PHM's first intron; the sites make different contributions to the total activity. These data suggest a model whereby the three E boxes interact cooperatively and independently to produce high PHM transcriptional activation. This DIMM-controlled PHM regulatory region displayed similar properties in vivo. Spatially, its expression mirrored that of the DIMM protein, and its activity was largely dependent on dimm. Further, in vivo expression was highly dependent on the sequences of the same three E boxes. This study supports the hypothesis that DIMM is a master regulator of a peptidergic cell fate in Drosophila and provides a detailed transcriptional mechanism of DIMM action on a defined target gene.

* Corresponding author. Mailing address: Department of Anatomy and Neurobiology, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110. Phone: (314) 362-3641. Fax: (314) 362-3446. E-mail: taghertp{at}pcg.wustl.edu

{triangledown} Published ahead of print on 29 October 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, January 2008, p. 410-421, Vol. 28, No. 1
0270-7306/08/$08.00+0     doi:10.1128/MCB.01104-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yoshii, T., Wulbeck, C., Sehadova, H., Veleri, S., Bichler, D., Stanewsky, R., Helfrich-Forster, C. (2009). The Neuropeptide Pigment-Dispersing Factor Adjusts Period and Phase of Drosophila's Clock. J. Neurosci. 29: 2597-2610 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»