scholarly journals Isolation of Alcohol Dehydrogenase cDNA and Basal Regulatory Region from Metroxylon sagu

2012 ◽  
Vol 2012 ◽  
pp. 1-9
Author(s):  
Ching Ching Wee ◽  
Hairul Azman Roslan
Keyword(s):  
Amino Acids ◽  
Alcohol Dehydrogenase ◽  
Elaeis Guineensis ◽  
Regulatory Region ◽  
Putative Promoter Region ◽  
Sago Palm ◽  
Binding Domains ◽  
Genomic Walking ◽  
Rapid Amplification ◽  
Metroxylon Sagu

Alcohol dehydrogenase (Adh) is a versatile enzyme involved in many biochemical pathways in plants such as in germination and stress tolerance. Sago palm is plant with much importance to the state of Sarawak as one of the most important crops that bring revenue with the advantage of being able to withstand various biotic and abiotic stresses such as heat, pathogens, and water logging. Here we report the isolation of sago palm Adh cDNA and its putative promoter region via the use of rapid amplification of cDNA ends (RACE) and genomic walking. The isolated cDNA was characterized and determined to be 1464 bp long encoding for 380 amino acids. BLAST analysis showed that the Adh is similar to the Adh1 group with 91% and 85% homology with Elaeis guineensis and Washingtonia robusta, respectively. The putative basal msAdh1 regulatory region was further determined to contain promoter signals of TATA and AGGA boxes and predicted amino acids analyses showed several Adh-specific motifs such as the two zinc-binding domains that bind to the adenosine ribose of the coenzyme and binding to alcohol substrate. A phylogenetic tree was also constructed using the predicted amino acid showed clear separation of Adh from bacteria and clustered within the plant Adh group.

Rhynchophorus palmarum. [Distribution map].

2006 ◽  
Author(s):  
Keyword(s):  
Elaeis Guineensis ◽  
Cocos Nucifera ◽  
Phoenix Dactylifera ◽  
Saccharum Officinarum ◽  
Distribution Map ◽  
Mato Grosso ◽  
Sago Palm ◽  
Rhynchophorus Palmarum ◽  
Metroxylon Sagu ◽  
Mato Grosso Do Sul

Abstract A revised distribution map is provided for Rhynchophorus palmarum (Linnaeus). Coleoptera: Dryophthoridae. Hosts: African oil palm (Elaeis guineensis), coconut (Cocos nucifera), date palm (Phoenix dactylifera), sago palm (Metroxylon sagu) and sugarcane (Saccharum officinarum). Information is given on the geographical distribution in North America (Mexico), Central America and Caribbean (Barbados, Belize, Costa Rica, Cuba, Dominica, Dominican Republic, El Salvador, Grenada, Guadeloupe, Guatemala, Honduras, Martinique, Nicaragua, Panama, Puerto Rico, St Lucia, St Vincent and the Grenadines, Trinidad and Tobago), South America (Argentina, Bolivia, Brazil, Amazonas, Bahia, Maranhao, Mato Grosso do Sul, Minas Gerais, Para, Pernambuco, Piaui, Rio de Janeiro, Rio Grande do Sul, Sao Paulo, Colombia, Ecuador, French Guiana, Guyana, Paraguay, Peru, Suriname, Uruguay, Venezuela).

scholarly journals Photosynthesis of Sago Palm (Metroxylon sagu Rottb.) Seedling at Different Air Temperatures

Agriculture ◽  
2018 ◽  
Vol 8 (1) ◽  
pp. 4 ◽  
Author(s):  
Aidil Azhar ◽  
Daigo Makihara ◽  
Hitoshi Naito ◽  
Hiroshi Ehara
Keyword(s):  
Sago Palm ◽  
Air Temperatures ◽  
Metroxylon Sagu

scholarly journals Differential Metabolites Markers from Trunking and Stressed NonTrunking Sago Palm (Metroxylon sagu Rottb.)

2020 ◽  
Vol 14 ◽  
Author(s):  
Hasnain Hussain ◽  
Wei-Jie Yan ◽  
Zainab Ngaini ◽  
Norzainizul Julaihi ◽  
Rina Tommy ◽  
...  
Keyword(s):  
Extraction Method ◽  
Methanol Extract ◽  
Economic Value ◽  
Principal Component ◽  
Leaf Extracts ◽  
Sulfurous Acid ◽  
Sago Palm ◽  
Hexyl Ester ◽  
Metroxylon Sagu ◽  
Metabolite Markers

Background: Sago palm is an important agricultural starch-producing crop in Malaysia. The trunk of sago palm is responsible for the production of the starch reaching maturity for harvesting after ten years. However, there are sago palms that failed to develop its trunk after 17 years being planted. This is known as a stressed “non-trunking” sago palm, which eliminates the economic value of the palms. Objective: The study was initiated to compare the differences in metabolite expression between trunking and non-trunking sago palm and secondly to determine the potential metabolite-makers that are related to differential phenotypes of sago palms. Method: Metabolites were extracted using various solvents and analysed using NMR spectroscopy and GC-MS spectrometry. Data obtained were subjected to principal component analysis. Results: The study determined that differential metabolites expression were detected in the leaf extracts of normal trunking sago palm compared to the non-trunking palms. Metabolite groups which are differently expressed between trunking and non-trunking sago palm are oils and waxes, haloalkanes, sulfite esters, phosphonates, phosphoric acid, thiophene ester, terpenes and tocopherols. GC-MS analysis of Jones & Kinghorn extraction method determined two sets of metabolite markers which explains the differences in metabolites expression of trunking and non-trunking sago palm in ethyl acetate and methanol extract of 89.55% comprising sulfurous ester compounds and 87.04% comprising sulfurous ester, sulfurous acid and cyclohexylmethyl hexyl ester respectively. Conclusion: Two sets of metabolite markers were expressed in the trunking and non-trunking sago palm. These metabolites can potentially be used as markers for identifying normal and stressed plants.

Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane

2002 ◽  
Vol 115 (8) ◽  
pp. 1583-1590 ◽  
Author(s):  
Angela I. M. Barth ◽  
Kathleen A. Siemers ◽  
W. James Nelson
Keyword(s):  
Amino Acids ◽  
Cluster Formation ◽  
Adenomatous Polyposis ◽  
Polyposis Coli ◽  
Binding Domains ◽  
C Terminus ◽  
Endogenous Proteins ◽  
Apc Protein ◽  
Necessary And Sufficient ◽  
Armadillo Repeats

End-binding protein (EB) 1 binds to the C-terminus of adenomatous polyposis coli (APC) protein and to the plus ends of microtubules (MT) and has been implicated in the regulation of APC accumulation in cortical clusters at the tip of extending membranes. We investigated which APC domains are involved in cluster localization and whether binding to EB1 or MTs is essential for APC cluster localization. Armadillo repeats of APC that lack EB1- and MT-binding domains are necessary and sufficient for APC localization in cortical clusters; an APC fragment lacking the armadillo repeats, but containing MT-and EB1-binding domains, does not localize to the cortical clusters but instead co-aligns with MTs throughout the cell. Significantly, analysis of endogenous proteins reveals that EB1 does not accumulate in the APC clusters. However, overexpressed EB1 does accumulate in APC clusters; the APC-binding domain in EB1 is located in the C-terminal region of EB1 between amino acids 134 and 268. Overexpressed APC- or MT-binding domains of EB1 localize to APC cortical clusters and MT, respectively, without affecting APC cluster formation itself. These results show that localization of APC in cortical clusters is different from that of EB1 at MT plus ends and appears to be independent of EB1.

scholarly journals Identification of the Nuclear Export Signal and STAT-Binding Domains of the Nipah Virus V Protein Reveals Mechanisms Underlying Interferon Evasion

2004 ◽  
Vol 78 (10) ◽  
pp. 5358-5367 ◽  
Author(s):  
Jason J. Rodriguez ◽  
Cristian D. Cruz ◽  
Curt M. Horvath
Keyword(s):  
Amino Acids ◽  
Protein Interactions ◽  
Nuclear Export ◽  
Nipah Virus ◽  
Nuclear Export Signal ◽  
Hendra Virus ◽  
Nuclear Accumulation ◽  
V Protein ◽  
Binding Domains ◽  
Export Signal

ABSTRACT The V proteins of Nipah virus and Hendra virus have been demonstrated to bind to cellular STAT1 and STAT2 proteins to form high-molecular-weight complexes that inhibit interferon (IFN)-induced antiviral transcription by preventing STAT nuclear accumulation. Analysis of the Nipah virus V protein has revealed a region between amino acids 174 and 192 that functions as a CRM1-dependent nuclear export signal (NES). This peptide is sufficient to complement an export-defective human immunodeficiency virus Rev protein, and deletion and substitution mutagenesis revealed that this peptide is necessary for both V protein shuttling and cytoplasmic retention of STAT1 and STAT2 proteins. However, the NES is not required for V-dependent IFN signaling inhibition. IFN signaling is blocked primarily by interaction between Nipah virus V residues 100 to 160 and STAT1 residues 509 to 712. Interaction with STAT2 requires a larger Nipah virus V segment between amino acids 100 and 300, but deletion of residues 230 to 237 greatly reduced STAT2 coprecipitation. Further, V protein interactions with cellular STAT1 is a prerequisite for STAT2 binding, and sequential immunoprecipitations demonstrate that V, STAT1, and STAT2 can form a tripartite complex. These findings characterize essential regions for Henipavirus V proteins that represent potential targets for therapeutic intervention.

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