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Pax proteins play a diverse role in early animal development and contain the characteristic paired domain, consisting of two
conserved helix-turn-helix motifs. In many Pax proteins the paired domain is fused to a second DNA binding domain of the paired-like
homeobox family. By amino acid sequence alignments, secondary structure prediction, 3D-structure comparison, and phylogenetic
reconstruction, we analyzed the relationship between Pax proteins and members of the Tc1 family of transposases, which possibly
share a common ancestor with Pax proteins. We suggest that the DNA binding domain of an ancestral transposase (proto-Pax transposase)
was fused to a homeodomain shortly after the emergence of metazoans about one billion years ago. Using the transposase sequences
as an outgroup we reexamined the early evolution of the Pax proteins. Our novel evolutionary scenario features a single homeobox
capturing event and an early duplication of Pax genes before the divergence of porifera, indicating a more diverse role of
Pax proteins in primitive animals than previously expected.
Received: 16 February 2000 / Accepted: 13 August 2000 相似文献
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Yi-Ting Wang Yu-Jiao Pan Chao-Cheng Cho Bo-Chi Lin Li-Hsin Su Yu-Chang Huang Chin-Hung Sun 《The Journal of biological chemistry》2010,285(42):32213-32226
Giardia lamblia differentiates into infectious cysts to survive outside of the host. It is of interest to identify factors involved in up-regulation of cyst wall proteins (CWPs) during this differentiation. Pax proteins are important regulators of development and cell differentiation in Drosophila and vertebrates. No member of this gene family has been reported to date in yeast, plants, or protozoan parasites. We have identified a pax-like gene (pax1) encoding a putative paired domain in the G. lamblia genome. Epitope-tagged Pax1 localized to nuclei during both vegetative growth and encystation. Recombinant Pax1 specifically bound to the AT-rich initiator elements of the encystation-induced cwp1 to -3 and myb2 genes. Interestingly, overexpression of Pax1 increased cwp1 to -3 and myb2 gene expression and cyst formation. Deletion of the C-terminal paired domain or mutation of the basic amino acids of the paired domain resulted in a decrease of the transactivation function of Pax1. Our results indicate that the Pax family has been conserved during evolution, and Pax1 could up-regulate the key encystation-induced genes to regulate differentiation of the protozoan eukaryote, G. lamblia. 相似文献
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