Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-4

codon; 797Em, ASH2P mutated in the E-box 791–797 bp upstream from the start codon; 194&797Em, ASH2P mutated in both of the E-boxes. Forks show the mutated E-box site (A). B, C, D and E are the results co-transfected of promoters and da with ASH1, ASH2, ASH3 and ase, respectively. E-boxes mutation significantly reduced the promoter activity in B, C and D (< 0.01), but had no effect in E (> 0.05).<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-8

loop domain, and a conserved C-terminal 16–17 aa motif also exists in each of the proneural genes but neither of the genes. Moreover, a conserved short motif SPxxS is also found in all of the investigated proteins. Amino acids that are similar in 100% of aligned sequences are shaded blue, in more than 80% but less than 100% with pink, and in more than 60% but less than 80% with darkgreen.<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-9

Tters upside of the branch lines show the duplication events as clarified by Wheeler et al. [16] (see discussion for detailed description). It is obvious that all of the Asense proteins are grouped to one clade and the proneural genes are grouped to another within the insect group. Bm-ASH2 and Bm-ASH3 are grouped to a sub-clade parallel the one which Bm-ASH1 is sorted in. Ag-ASH, Achaete-Scute homolog (Genbank: ); Am-ASH,Achaete-Scute homolog (Genbank: ); B-ASH1, Butterfly (Genbank: ) Achaete-Scute homolog 1 (Genbank: ); Bm-ASH1, Achaete-Scute homolog 1 (Genbank: ); Bm-ASH2, Achaete-Scute homolog 2 (Genbank: ); Bm-ASH3, Achaete-Scute homolog 3 (Genbank: ); Cn-ASH, Achaete-Scute homolog (Genbank: ); Cs-ASH1, Achaete-Scute homolog 1 (Genbank: ); Cs-ASH2, Achaete-Scute homolog 2 (Genbank: ); Dm-ac, Achaete (Genbank: ); Dm-sc, Scute (Genbank: ); Dm-l'sc, Lethal of scute (Genbank: ); Pc-ASH1, Achaete-Scute homolog 1 (Genbank: ); Tc-ASH, Achaete-Scute homolog (Genbank: ); Ag-ase, Asense (Genbank: ); Am-ase, Asense (Genbank: ); Bm-ase, Asense (Genbank: ); Dm-ase, Asense (Genbank: ); Tc-ase, Asense (Genbank: ).<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-5

tubule), TC (trachea cluster), BW (body wall); mesoderm tissues He (hemocyte), FB (fat body), G (gonad, T (testis), O (ovary)); and endoderm tissue MG (midgut). V3d stands for 3-day-old larvae of the 5th instar, and S stands for 8-day-old larvae of the 5th instar (begin spinning). Amplification cycles were 30 for , , and , and 25 for the internal control gene .<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-0

and specification of the Q-PCR are good.<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-2

genomic DNA; (+) and (-) show the published genomic sequences [39] being forward or reverse compared with the cDNAs. "?" shows the region unsequenced. The 6 bp in indicates that there is a 6 bp uncoding region in the first exon of the gene just following the coding region, so is the 4 bp in . Genomic sequences are all from SilkDB [39]. The name of the genomic DNA fragment in is Scaffold002070, in is Scaffold007910, in is Scaffold013050, and in is Scaffold000880, respectively.<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-6

Carried out for each developmental stage.<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family-3

A respectively stands for the modified transient expression vector pBacPAK8-ie1-hr3 containing , , , and () ORFs as transcriptional factor genes. At least three independent repeats were carried out for each treatment.<p><b>Copyright information:</b></p><p>Taken from "Analysis of four homologs in reveals new viewpoints of the evolution and functions of this gene family"</p><p>http://www.biomedcentral.com/1471-2156/9/24</p><p>BMC Genetics 2008;9():24-24.</p><p>Published online 6 Mar 2008</p><p>PMCID:PMC2315653.</p><p></p

Characterization and expression patterns of a membrane-bound trehalase from -1

(), (), (), (), (), (), (), () and () using Vector NTI 9.0 multiple sequence alignment software. Highly conserved regions are highlighted in yellow and blue.<p><b>Copyright information:</b></p><p>Taken from "Characterization and expression patterns of a membrane-bound trehalase from "</p><p>http://www.biomedcentral.com/1471-2199/9/51</p><p>BMC Molecular Biology 2008;9():51-51.</p><p>Published online 20 May 2008</p><p>PMCID:PMC2424068.</p><p></p

Characterization and expression patterns of a membrane-bound trehalase from -7

L peptide and putative cleavage site, respectively. Trehalase signature motifs (amino acid residues 165–178 and 466–475) are double underlined. The highly conserved glycine-rich region is shaded. The putative transmembrane region (residues 585–607) is shaded and boxed. Potential N-glycosylation sites (amino acid residues 49, 64, 261, 331, 337 and 419) are boxed. The nucleotide sequence reported in this paper has been submitted to GenBank under accession number .<p><b>Copyright information:</b></p><p>Taken from "Characterization and expression patterns of a membrane-bound trehalase from "</p><p>http://www.biomedcentral.com/1471-2199/9/51</p><p>BMC Molecular Biology 2008;9():51-51.</p><p>Published online 20 May 2008</p><p>PMCID:PMC2424068.</p><p></p