Genome Research scroll

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fassler, J.
Right arrow Articles by Vinson, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fassler, J.
Right arrow Articles by Vinson, C.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Vol. 12, Issue 8, 1190-1200, August 2002

LETTER
B-ZIP Proteins Encoded by the Drosophila Genome: Evaluation of Potential Dimerization Partners

Jan Fassler,1,3 David Landsman,1 Asha Acharya,2 Jonathan R. Moll,2 Maria Bonovich,2 and Charles Vinson2,4

1 Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20814, USA; 2 Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA; 3 Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242, USA

The basic region-leucine zipper (B-ZIP) (bZIP) protein motif dimerizes to bind specific DNA sequences. We have identified 27 B-ZIP proteins in the recently sequenced Drosophila melanogaster genome. The dimerization specificity of these 27 B-ZIP proteins was evaluated using two structural criteria: (1) the presence of attractive or repulsive interhelical gleft-right-arrowe` electrostatic interactions and (2) the presence of polar or charged amino acids in the `a' and `d' positions of the hydrophobic interface. None of the B-ZIP proteins contain only aliphatic amino acids in the`a' and `d' position. Only six of the Drosophila B-ZIP proteins contain a "canonical" hydrophobic interface like the yeast GCN4, and the mammalian JUN, ATF2, CREB, C/EBP, and PAR leucine zippers, characterized by asparagine in the second `a' position. Twelve leucine zippers contain polar amino acids in the first, third, and fourth `a' positions. Circular dichroism spectroscopy, used to monitor thermal denaturations of a heterodimerizing leucine zipper system containing either valine (V) or asparagine (N) in the `a' position, indicates that the V-N interaction is 2.3 kcal/mole less stable than an N-N interaction and 5.3 kcal/mole less stable than a V-V interaction. Thus, we propose that the presence of polar amino acids in novel positions of the `a' position of Drosophila B-ZIP proteins has led to leucine zippers that homodimerize rather than heterodimerize.


4 Corresponding author.


12:1190-1200 ©2002 by Cold Spring Harbor Laboratory Press  ISSN 1088-9051/02 $5.00

Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Plant Physiol.Home page
A. Nijhawan, M. Jain, A. K. Tyagi, and J. P. Khurana
Genomic Survey and Gene Expression Analysis of the Basic Leucine Zipper Transcription Factor Family in Rice
Plant Physiology, February 1, 2008; 146(2): 333 - 350.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
G. Amoutzias, A. Veron, J Weiner III, M Robinson-Rechavi, E Bornberg-Bauer, S. Oliver, and D. Robertson
One Billion Years of bZIP Transcription Factor Evolution: Conservation and Change in Dimerization and DNA-Binding Site Specificity
Mol. Biol. Evol., March 1, 2007; 24(3): 827 - 835.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
F. Meyer, S. Perez, V. Geiser, M. Sintek, M. Inman, and C. Jones
A Protein Encoded by the Bovine Herpesvirus 1 Latency-Related Gene Interacts with Specific Cellular Regulatory Proteins, Including CCAAT Enhancer Binding Protein Alpha
J. Virol., January 1, 2007; 81(1): 59 - 67.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
C. D. Deppmann, R. S. Alvania, and E. J. Taparowsky
Cross-Species Annotation of Basic Leucine Zipper Factor Interactions: Insight into the Evolution of Closed Interaction Networks
Mol. Biol. Evol., August 1, 2006; 23(8): 1480 - 1492.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
A. V. McDonnell, T. Jiang, A. E. Keating, and B. Berger
Paircoil2: improved prediction of coiled coils from sequence
Bioinformatics, February 1, 2006; 22(3): 356 - 358.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
C. D. Deppmann, A. Acharya, V. Rishi, B. Wobbes, S. Smeekens, E. J. Taparowsky, and C. Vinson
Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a comparison to Homo sapiens B-ZIP motifs
Nucleic Acids Res., June 29, 2004; 32(11): 3435 - 3445.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
K.-I. Nonomura, M. Nakano, T. Fukuda, M. Eiguchi, A. Miyao, H. Hirochika, and N. Kurata
The Novel Gene HOMOLOGOUS PAIRING ABERRATION IN RICE MEIOSIS1 of Rice Encodes a Putative Coiled-Coil Protein Required for Homologous Chromosome Pairing in Meiosis
PLANT CELL, April 1, 2004; 16(4): 1008 - 1020.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
K. A. Borkovich, L. A. Alex, O. Yarden, M. Freitag, G. E. Turner, N. D. Read, S. Seiler, D. Bell-Pedersen, J. Paietta, N. Plesofsky, et al.
Lessons from the Genome Sequence of Neurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism
Microbiol. Mol. Biol. Rev., March 1, 2004; 68(1): 1 - 108.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Genes Dev. Learn. Mem.
Protein Science RNA Genome Res.