The Drosophila homeobox gene optix is capable of inducing ectopic eyes by an eyeless-independent mechanism

Development ◽  
2000 ◽  
Vol 127 (9) ◽  
pp. 1879-1886 ◽  
Author(s):  
M. Seimiya ◽  
W.J. Gehring
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Family ◽  
Eye Development ◽  
Ectopic Expression ◽  
Amino Acid Sequence Similarity ◽  
Sine Oculis ◽  
High Amino Acid ◽  
Independent Mechanism ◽  
Ectopic Eyes

optix is a new member of the Six/so gene family from Drosophila that contains both a six domain and a homeodomain. Because of its high amino acid sequence similarity with the mouse Six3 gene, optix is considered to be the orthologous gene from Drosophila rather than sine oculis, as previously believed. optix expression was detected in the eye, wing and haltere imaginal discs. Ectopic expression of optix leads to the formation of ectopic eyes suggesting that optix has important functions in eye development. Although optix and sine oculis belong to the same gene family (Six/so) and share a high degree of amino acid sequence identity, there are a number of factors which suggest that their developmental roles are different: (1) the expression patterns of optix and sine oculis are clearly distinct; (2) sine oculis acts downstream of eyeless, whereas optix is expressed independently of eyeless; (3) sine oculis functions synergistically with eyes absent in eye development whereas optix does not; (4) ectopic expression of optix alone, but not of sine oculis can induce ectopic eyes in the antennal disc. These results suggest that optix is involved in eye morphogenesis by an eyeless-independent mechanism.

Characterization of new fungal carbohydrate esterase family 1 proteins leads to the discovery of two novel dual feruloyl/acetyl xylan esterases

2020 ◽  
Author(s):  
Adiphol Dilokpimol ◽  
Bart Verkerk ◽  
Annie Bellemare ◽  
Mathieu Lavallee ◽  
Matthias Frommhagen ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ferulic Acid ◽  
Plant Cell Wall ◽  
Plant Biomass ◽  
Amino Acid Sequence Similarity ◽  
Carbohydrate Esterase ◽  
Wheat Arabinoxylan ◽  
High Amino Acid

Abstract Background Feruloyl esterases (FAEs) and acetyl xylan esterases (AXEs) are important accessory enzymes in the deconstruction of plant biomass. Carbohydrate Esterase family 1 (CE1) of the Carbohydrate-Active enZymes database contains both fungal FAEs and AXEs, sharing a high amino acid sequence similarity, even though they target different structural molecules on plant cell wall polysaccharides. Results We recently classified fungal CE1 into five subfamilies (CE1_SF1-5). In this study, ten novel fungal CE1 enzymes from different subfamilies were heterologously produced in Aspergillus niger and characterized to gain insight on relationships among these esterases. The enzymes from CE1_SF1 possess AXE activity, as they hydrolyzed p NP-acetate and released acetic acid from wheat arabinoxylan, but were not active towards FAE substrates. CE1_SF5 showed FAE activity as they hydrolyzed methyl ferulate and other FAE related substrates, and release ferulic acid from wheat arabinoxylan. These FAEs preferred feruloylated arabinoxylan over pectin. Two CE1_SF2, sharing over 70% amino acid sequence identity, possessed the opposite activity. Interestingly, one enzyme from CE1_SF1 and one from CE1_SF5 possess dual feruloyl/acetyl xylan esterase (FXE) activity. These dual activity enzymes showed expansion of substrate specificity. Conclusions The new FXEs from CE1 can efficiently release both ferulic acid and acetic acid from feruloylated xylan, making them particularly interesting novel components of industrial enzyme cocktails for plant biomass degradation.

scholarly journals Engineered Resistance Against Papaya ringspot virus in Venezuelan Transgenic Papayas

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Agrobacterium Tumefaciens ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Ringspot Virus ◽  
Amino Acid Sequence Similarity ◽  
Papaya Ringspot Virus ◽  
Local Varieties ◽  
Cp Gene

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.

scholarly journals NoPv1: a synthetic antimicrobial peptide aptamer targeting the causal agents of grapevine downy mildew and potato late blight

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Monica Colombo ◽  
Simona Masiero ◽  
Stefano Rosa ◽  
Elisabetta Caporali ◽  
Silvia Laura Toffolatti ◽  
...  
Keyword(s):  
Amino Acid ◽  
Late Blight ◽  
Downy Mildew ◽  
Negative Impact ◽  
Hybrid Approach ◽  
Cellulose Synthase ◽  
Economic Losses ◽  
Amino Acid Sequence Similarity ◽  
High Amino Acid ◽  
Peptide Aptamer

Abstract Grapevine (Vitis vinifera L.) is a crop of major economic importance. However, grapevine yield is guaranteed by the massive use of pesticides to counteract pathogen infections. Under temperate-humid climate conditions, downy mildew is a primary threat for viticulture. Downy mildew is caused by the biotrophic oomycete Plasmopara viticola Berl. & de Toni, which can attack grapevine green tissues. In lack of treatments and with favourable weather conditions, downy mildew can devastate up to 75% of grape cultivation in one season and weaken newly born shoots, causing serious economic losses. Nevertheless, the repeated and massive use of some fungicides can lead to environmental pollution, negative impact on non-targeted organisms, development of resistance, residual toxicity and can foster human health concerns. In this manuscript, we provide an innovative approach to obtain specific pathogen protection for plants. By using the yeast two-hybrid approach and the P. viticola cellulose synthase 2 (PvCesA2), as target enzyme, we screened a combinatorial 8 amino acid peptide library with the aim to identify interacting peptides, potentially able to inhibit PvCesa2. Here, we demonstrate that the NoPv1 peptide aptamer prevents P. viticola germ tube formation and grapevine leaf infection without affecting the growth of non-target organisms and without being toxic for human cells. Furthermore, NoPv1 is also able to counteract Phytophthora infestans growth, the causal agent of late blight in potato and tomato, possibly as a consequence of the high amino acid sequence similarity between P. viticola and P. infestans cellulose synthase enzymes.

scholarly journals High-Efficiency Utilization of the Bovine Integrin αvβ3 as a Receptor for Foot-and-Mouth Disease Virus Is Dependent on the Bovine β3Subunit

2000 ◽  
Vol 74 (16) ◽  
pp. 7298-7306 ◽  
Author(s):  
Sherry Neff ◽  
Peter W. Mason ◽  
Barry Baxt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disease Virus ◽  
Sequence Similarity ◽  
Foot And Mouth Disease ◽  
Viral Proteins ◽  
Mouth Disease ◽  
Amino Acid Sequence Similarity ◽  
Mouth Disease Virus ◽  
Human Integrin

ABSTRACT We have previously reported that Foot-and-mouth disease virus (FMDV), which is virulent for cattle and swine, can utilize the integrin αvβ3 as a receptor on cultured cells. Since those studies were performed with the human integrin, we have molecularly cloned the bovine homolog of the integrin αvβ3 and have compared the two receptors for utilization by FMDV. Both the αv and β3subunits of the bovine integrin have high degrees of amino acid sequence similarity to their corresponding human subunits in the ectodomains (96%) and essentially identical transmembrane and cytoplasmic domains. Within the putative ligand-binding domains, the bovine and human αv subunits have a 98.8% amino acid sequence similarity while there is only a 93% similarity between the β3 subunits of these two species. COS cell cultures, which are not susceptible to FMDV infection, become susceptible if cotransfected with αv and β3 subunit cDNAs from a bovine or human source. Cultures cotransfected with the bovine αvβ3 subunit cDNAs and infected with FMDV synthesize greater amounts of viral proteins than do infected cultures cotransfected with the human integrin subunits. Cells cotransfected with a bovine αv subunit and a human β3subunit synthesize viral proteins at levels equivalent to those in cells expressing both human subunits. However, cells cotransfected with the human αv and the bovine β3 subunits synthesize amounts of viral proteins equivalent to those in cells expressing both bovine subunits, indicating that the bovine β3 subunit is responsible for the increased effectiveness of this receptor. By engineering chimeric bovine-human β3subunits, we have shown that this increase in receptor efficiency is due to sequences encoding the C-terminal one-third of the subunit ectodomain, which contains a highly structured cysteine-rich repeat region. We postulate that amino acid sequence differences within this region may be responsible for structural differences between the human and bovine β3 subunit, leading to more efficient utilization of the bovine receptor by this bovine pathogen.

scholarly journals Inhibition of mitogen-activated protein kinase by a Drosophila dual-specific phosphatase

2000 ◽  
Vol 349 (3) ◽  
pp. 821-828 ◽  
Author(s):  
Won-Jae LEE ◽  
Sun-Hong KIM ◽  
Yong-Sik KIM ◽  
Sung-Jun HAN ◽  
Ki-Sook PARK ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Expressed Sequence Tag ◽  
Mapk Pathway ◽  
Sequence Similarity ◽  
Mitogen Activated Protein Kinase ◽  
Amino Acid Sequence Similarity ◽  
Calculated Molecular Mass ◽  
High Amino Acid ◽  
Mitogen Activated Protein

The Drosophila extracellular signal-regulated kinase (DERK) mitogen-activated protein kinase (MAPK) is involved in the regulation of multiple differentiation and developmental processes. Tight control of MAPK activity is critical for normal cell behaviour. We identified a novel Drosophila MAPK phosphatase (DMKP) cDNA from the expressed-sequence-tag database and characterized it. Analysis of the nucleotide sequence revealed an open reading frame encoding the 203-amino acid protein, with a calculated molecular mass of 23kDa, which has a high amino acid sequence similarity with ‘VH1-like’dual-specific phosphatases at the broad region near the catalytic sites. The expression of DMKP mRNA occurs from the late larval stages to adulthood in Drosophila development. The recombinant DMKP protein produced in yeast retained its phosphatase activity. When expressed in Schneider cells, DMKP dose-dependently inhibited DERK and Drosophila c-Jun N-terminal kinase activities with high selectivity towards DERK. However, DMKP did not have any affect on Drosophila p38 activity. When DMKP was expressed in yeast, it down-regulated the fus1-lacZ trans-reporter gene of the pheromone MAPK pathway without any significant effect on the high-osmolarity-glycerol-response pathway.

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