Phosphorylation, expression and function of the Ultrabithorax protein family in Drosophila melanogaster - PubMed (original) (raw)
. 1991 Aug;112(4):1077-93.
doi: 10.1242/dev.112.4.1077.
Affiliations
- PMID: 1682129
- DOI: 10.1242/dev.112.4.1077
Phosphorylation, expression and function of the Ultrabithorax protein family in Drosophila melanogaster
E R Gavis et al. Development. 1991 Aug.
Abstract
Alternative splicing of the Ultrabithorax homeotic gene transcript generates a family of five proteins (UBX isoforms) that function as transcription factors. All isoforms contain a homeodomain within a common 99 aa C-terminal region (C-constant region) which is jointed to a common 247 aa N-terminal (N-constant) region by different combinations of three small optional elements. Unlike the UBX proteins expressed in E. coli, UBX isoforms expressed in D. melanogaster cells are phosphorylated on serine and threonine residues, located primarily within a 53 aa region near the middle of the N-constant region, to form at least five phosphorylated states per isoform. Similar, if not identical states can be generated in vitro from purified E. coli UBX protein by a kinase activity in nuclear extracts from D. melanogaster cells. Temporal developmental profiles of UBX isoforms parallel those for the respective mRNAs, and all isoforms are similarly phosphorylated throughout embryogenesis. Analysis by cotransfection assays of the promoter activation and repression functions of mutant UBX proteins with various deletions in the N-constant region shows that repression is generally insensitive to deletion and, hence, presumably to phosphorylation. By contrast, the activation function is differentially sensitive to the different deletions in a manner indicating the absence of a discrete activating domain and instead, the presence of multiple activating sequences spread throughout the region.
Similar articles
- Evolutionary conservation of the structure and expression of alternatively spliced Ultrabithorax isoforms from Drosophila.
Bomze HM, López AJ. Bomze HM, et al. Genetics. 1994 Mar;136(3):965-77. doi: 10.1093/genetics/136.3.965. Genetics. 1994. PMID: 7911773 Free PMC article. - Transcriptional activation and repression by Ultrabithorax proteins in cultured Drosophila cells.
Krasnow MA, Saffman EE, Kornfeld K, Hogness DS. Krasnow MA, et al. Cell. 1989 Jun 16;57(6):1031-43. doi: 10.1016/0092-8674(89)90341-3. Cell. 1989. PMID: 2567632 - Immunochemical dissection of the Ultrabithorax homeoprotein family in Drosophila melanogaster.
Lopez AJ, Hogness DS. Lopez AJ, et al. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):9924-8. doi: 10.1073/pnas.88.22.9924. Proc Natl Acad Sci U S A. 1991. PMID: 1719557 Free PMC article. - Roles for intrinsic disorder and fuzziness in generating context-specific function in Ultrabithorax, a Hox transcription factor.
Bondos SE, Hsiao HC. Bondos SE, et al. Adv Exp Med Biol. 2012;725:86-105. doi: 10.1007/978-1-4614-0659-4_6. Adv Exp Med Biol. 2012. PMID: 22399320 Review.
Cited by
- Post-translational modifications of Drosophila melanogaster HOX protein, Sex combs reduced.
Banerjee A, Percival-Smith A. Banerjee A, et al. PLoS One. 2020 Jan 13;15(1):e0227642. doi: 10.1371/journal.pone.0227642. eCollection 2020. PLoS One. 2020. PMID: 31931520 Free PMC article. - Evidence for a Strong Correlation Between Transcription Factor Protein Disorder and Organismic Complexity.
Yruela I, Oldfield CJ, Niklas KJ, Dunker AK. Yruela I, et al. Genome Biol Evol. 2017 May 1;9(5):1248-1265. doi: 10.1093/gbe/evx073. Genome Biol Evol. 2017. PMID: 28430951 Free PMC article. - Mechanisms of Specificity for Hox Factor Activity.
Zandvakili A, Gebelein B. Zandvakili A, et al. J Dev Biol. 2016 Jun;4(2):16. doi: 10.3390/jdb4020016. Epub 2016 May 9. J Dev Biol. 2016. PMID: 27583210 Free PMC article. - Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox Proteins.
Bondos SE, Swint-Kruse L, Matthews KS. Bondos SE, et al. J Biol Chem. 2015 Oct 9;290(41):24669-77. doi: 10.1074/jbc.R115.685032. Epub 2015 Sep 4. J Biol Chem. 2015. PMID: 26342073 Free PMC article. Review. - Rethinking gene regulatory networks in light of alternative splicing, intrinsically disordered protein domains, and post-translational modifications.
Niklas KJ, Bondos SE, Dunker AK, Newman SA. Niklas KJ, et al. Front Cell Dev Biol. 2015 Feb 26;3:8. doi: 10.3389/fcell.2015.00008. eCollection 2015. Front Cell Dev Biol. 2015. PMID: 25767796 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous