scholarly journals Functional Characterization and Subcellular Localization of Poplar (Populus trichocarpa × Populus deltoides) Cinnamate 4-Hydroxylase

2001 ◽  
Vol 126 (1) ◽  
pp. 317-329 ◽  
Author(s):  
Dae Kyun Ro ◽  
Nancy Mah ◽  
Brian E. Ellis ◽  
Carl J. Douglas
Keyword(s):  
Subcellular Localization ◽  
Populus Deltoides ◽  
Populus Trichocarpa ◽  
Functional Characterization

Bt-Cry3Aa transgene expression reduces insect damage and improves growth in field-grown hybrid poplar

2014 ◽  
Vol 44 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Amy L. Klocko ◽  
Richard Meilan ◽  
Rosalind R. James ◽  
Venkatesh Viswanath ◽  
Cathleen Ma ◽  
...  
Keyword(s):  
Large Scale ◽  
Populus Deltoides ◽  
Integrated Management ◽  
Populus Trichocarpa ◽  
Hybrid Poplar ◽  
Volume Growth ◽  
Field Trials ◽  
Leaf Beetle ◽  
Insect Damage ◽  
Beetle Damage

The stability and value of transgenic pest resistance for promoting tree growth are poorly understood. These data are essential for determining if such trees could be beneficial to commercial growers in the face of substantial regulatory and marketing costs. We investigated growth and insect resistance in hybrid poplar expressing the cry3Aa transgene in two field trials. An initial screening of 502 trees comprising 51 transgenic gene insertion events in four clonal backgrounds (Populus trichocarpa × Populus deltoides, clones 24-305, 50-197, and 198-434; and P. deltoides × Populus nigra, clone OP-367) resulted in transgenic trees with greatly reduced insect damage. A large-scale study of 402 trees from nine insertion events in clone OP-367, conducted over two growing seasons, demonstrated reduced tree damage and significantly increased volume growth (mean 14%). Quantification of Cry3Aa protein indicated high levels of expression, which continued after 14 years of annual or biannual coppice in a clone bank. With integrated management, the cry3Aa gene appears to be a highly effective tool for protecting against leaf beetle damage and improving yields from poplar plantations.

scholarly journals Localization and function of a Plasmodium falciparum protein (PF3D7_1459400) during erythrocyte invasion

2020 ◽  
pp. 153537022096176
Author(s):  
Emmanuel Amlabu ◽  
Prince B Nyarko ◽  
Grace Opoku ◽  
Damata Ibrahim-Dey ◽  
Philip Ilani ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Subcellular Localization ◽  
Protein Expression ◽  
Functional Characterization ◽  
Blood Stage ◽  
Protein Subcellular Localization ◽  
Erythrocyte Invasion ◽  
Invasion Inhibition ◽  
Blood Stage Malaria ◽  
Peptide Antibodies

Nearly 60% of Plasmodium falciparum proteins are still uncharacterized and their functions are unknown. In this report, we carried out the functional characterization of a 45 kDa protein (PF3D7_1459400) and showed its potential as a target for blood stage malaria vaccine development. Analysis of protein subcellular localization, native protein expression profile, and erythrocyte invasion inhibition of both clinical and laboratory parasite strains by peptide antibodies suggest a functional role of PF3D7_1459400 protein during erythrocyte invasion. Also, immunoreactivity screens using synthetic peptides of the protein showed that adults resident in malaria endemic regions in Ghana have naturally acquired plasma antibodies against PF3D7_1459400 protein. Altogether, this study presents PF3D7_1459400 protein as a potential target for the development of peptide-based vaccine for blood-stage malaria. Impact statement Plasmodium falciparum malaria is a global health problem. Erythrocyte invasion by P. falciparum merozoites appears to be a promising target to curb malaria. We have identified and characterized a novel protein that is involved in erythrocyte invasion. Our data on protein subcellular localization, stage-specific protein expression pattern, and merozoite invasion inhibition by α-peptide antibodies suggest a role for PF3D7_1459400 protein during P. falciparum erythrocyte invasion. Even more, the human immunoepidemiology data present PF3D7_1459400 protein as an immunogenic antigen which could be further exploited for the development of new anti-infective therapy against malaria.

scholarly journals BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked exocytosis

2014 ◽  
Vol 205 (2) ◽  
pp. 233-249 ◽  
Author(s):  
Pascal Béguin ◽  
Kazuaki Nagashima ◽  
Ramasubbu N. Mahalakshmi ◽  
Réjan Vigot ◽  
Atsuko Matsunaga ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Functional Characterization ◽  
Regulatory Protein ◽  
Binding Pocket ◽  
Neuroendocrine Cells ◽  
Cell Surface Expression ◽  
Channel Activity ◽  
Interaction Domain ◽  
Voltage Gated ◽  
Domain I

Voltage-gated calcium channels (VGCCs) are key regulators of cell signaling and Ca2+-dependent release of neurotransmitters and hormones. Understanding the mechanisms that inactivate VGCCs to prevent intracellular Ca2+ overload and govern their specific subcellular localization is of critical importance. We report the identification and functional characterization of VGCC β-anchoring and -regulatory protein (BARP), a previously uncharacterized integral membrane glycoprotein expressed in neuroendocrine cells and neurons. BARP interacts via two cytosolic domains (I and II) with all Cavβ subunit isoforms, affecting their subcellular localization and suppressing VGCC activity. Domain I interacts at the α1 interaction domain–binding pocket in Cavβ and interferes with the association between Cavβ and Cavα1. In the absence of domain I binding, BARP can form a ternary complex with Cavα1 and Cavβ via domain II. BARP does not affect cell surface expression of Cavα1 but inhibits Ca2+ channel activity at the plasma membrane, resulting in the inhibition of Ca2+-evoked exocytosis. Thus, BARP can modulate the localization of Cavβ and its association with the Cavα1 subunit to negatively regulate VGCC activity.

scholarly journals Molecular Cloning, Functional Characterization, and Subcellular Localization of Soybean Nodule Dihydrolipoamide Reductase

2002 ◽  
Vol 128 (1) ◽  
pp. 300-313 ◽  
Author(s):  
Jose F. Moran ◽  
Zhaohui Sun ◽  
Gautam Sarath ◽  
Raúl Arredondo-Peter ◽  
Euan K. James ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Molecular Cloning ◽  
Functional Characterization ◽  
Soybean Nodule

scholarly journals Defining hybrid poplar (Populus deltoides × Populus trichocarpa) tolerance to ozone: identifying key parameters

2009 ◽  
Vol 32 (1) ◽  
pp. 31-45 ◽  
Author(s):  
A. RYAN ◽  
C. COJOCARIU ◽  
M. POSSELL ◽  
W. J. DAVIES ◽  
C. N. HEWITT
Keyword(s):  
Populus Deltoides ◽  
Populus Trichocarpa ◽  
Hybrid Poplar

Ion homeostasis, channels, and transporters: an update on cellular mechanisms

2004 ◽  
Vol 28 (4) ◽  
pp. 143-154 ◽  
Author(s):  
George R. Dubyak
Keyword(s):  
Ion Channels ◽  
Subcellular Localization ◽  
Ion Transport ◽  
Membrane Transport ◽  
Cell Biology ◽  
Functional Characterization ◽  
Transport Proteins ◽  
Transport Protein ◽  
Membrane Transport Proteins ◽  
Functional Analyses

The steady-state maintenance of highly asymmetric concentrations of the major inorganic cations and anions is a major function of both plasma membranes and the membranes of intracellular organelles. Homeostatic regulation of these ionic gradients is critical for most functions. Due to their charge, the movements of ions across biological membranes necessarily involves facilitation by intrinsic membrane transport proteins. The functional characterization and categorization of membrane transport proteins was a major focus of cell physiological research from the 1950s through the 1980s. On the basis of these functional analyses, ion transport proteins were broadly divided into two classes: channels and carrier-type transporters (which include exchangers, cotransporters, and ATP-driven ion pumps). Beginning in the mid-1980s, these functional analyses of ion transport and homeostasis were complemented by the cloning of genes encoding many ion channels and transporter proteins. Comparison of the predicted primary amino acid sequences and structures of functionally similar ion transport proteins facilitated their grouping within families and superfamilies of structurally related membrane proteins. Postgenomics research in ion transport biology increasingly involves two powerful approaches. One involves elucidation of the molecular structures, at the atomic level in some cases, of model ion transport proteins. The second uses the tools of cell biology to explore the cell-specific function or subcellular localization of ion transport proteins. This review will describe how these approaches have provided new, and sometimes surprising, insights regarding four major questions in current ion transporter research. 1) What are the fundamental differences between ion channels and ion transporters? 2) How does the interaction of an ion transport protein with so-called adapter proteins affect its subcellular localization or regulation by various intracellular signal transduction pathways? 3) How does the specific lipid composition of the local membrane microenvironment modulate the function of an ion transport protein? 4) How can the basic functional properties of a ubiquitously expressed ion transport protein vary depending on the cell type in which it is expressed?

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