The molecular mechanism underlying pathogenicity inhibition by sanguinarine in Magnaporthe oryzae

2021 ◽  
Author(s):  
Wilfred M. Anjago ◽  
Wenlong Zeng ◽  
Yixiao Chen ◽  
Yupeng Wang ◽  
Jules Biregeya ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Magnaporthe Oryzae

Unraveling the Molecular Mechanism of Magnaporthe oryzae Induced Signaling Cascade in Rice

2020 ◽  
pp. 363-377
Author(s):  
Nisha Khatri ◽  
Qingfeng Meng ◽  
Sun Tae Kim ◽  
Ravi Gupta
Keyword(s):  
Molecular Mechanism ◽  
Magnaporthe Oryzae ◽  
Signaling Cascade

scholarly journals Vacuolar transporter Mnr2 safeguards mitochondrial integrity in aged cells

2020 ◽  
Author(s):  
Md. Hashim Reza ◽  
Rajesh Patkar ◽  
Kaustuv Sanyal
Keyword(s):  
Cell Death ◽  
Molecular Mechanism ◽  
Magnaporthe Oryzae ◽  
Mitochondrial Function ◽  
Vacuolar Membrane ◽  
Ion Flux ◽  
Ion Transporter ◽  
Mitochondrial Structure ◽  
Mitochondrial Integrity ◽  
And Function

AbstractAging is associated with altered mitochondrial function. Mitochondrial function is dependent on the magnesium (Mg+2) ion flux. The molecular mechanism underlying Mg+2 homeostasis, especially during aging has not been well understood. We previously demonstrated that the absence of a vacuolar ion transporter Mnr2 accelerates cell death in the older part of the colony in Magnaporthe oryzae presumably due to an altered Mg+2 homeostasis. Localization of Mnr2 as dynamic puncta at the vacuolar membrane especially in the older Magnaporthe cells further suggests its association with aged cells. Interestingly, such vacuolar Mnr2 puncta colocalized with the filamentous mitochondria in the aged cells. Further, we show that aged mnr2Δ null cells displayed loss of integrity of mitochondria and vacuoles. Remarkably, exogenously added Mg+2 restored the mitochondrial structure as well as improved the lifespan of mnr2Δ null cells. Thus, we uncover a mechanism of maintenance of mitochondrial integrity and function by the ion transporter Mnr2-based Mg+2 homeostasis during aging.

Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1

2019 ◽  
Vol 476 (21) ◽  
pp. 3227-3240 ◽  
Author(s):  
Shanshan Wang ◽  
Yanxiang Zhao ◽  
Long Yi ◽  
Minghe Shen ◽  
Chao Wang ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Magnaporthe Oryzae ◽  
Structural Information ◽  
Complex Structure ◽  
Critical Role ◽  
Catalytic Process ◽  
Structural Basis ◽  
Salt Bridges ◽  
Terminal Domain

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

Additional evidence for AQP1 vesicle trafficking as a molecular mechanism for ductal bile secretion

2001 ◽  
Vol 120 (5) ◽  
pp. A91-A91
Author(s):  
P TIETZ ◽  
P SPLINTER ◽  
M MCNIVEN ◽  
R HUEBERT ◽  
N LARUSSO
Keyword(s):  
Molecular Mechanism ◽  
Vesicle Trafficking ◽  
Bile Secretion

Hypoxia/Reoxygenation on human myometrial and decidual cells: A molecular mechanism involved in preterra labor

1998 ◽  
Vol 5 (1) ◽  
pp. 187A-187A
Author(s):  
J CARVAJAL ◽  
S KATO ◽  
J SAEZ ◽  
F LEIGHTON ◽  
G VALENZUELA ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Decidual Cells ◽  
Hypoxia Reoxygenation

Molecular Mechanism of Apoptosis Induction by Resveratrol, a Natural Cancer Chemopreventive Agent

2008 ◽  
Vol 78 (1) ◽  
pp. 3-8 ◽  
Author(s):  
Fan ◽  
Jiang ◽  
Zhang ◽  
Bai
Keyword(s):  
Cancer Treatment ◽  
Molecular Mechanism ◽  
Apoptosis Induction ◽  
Protective Agents ◽  
Chemopreventive Agent ◽  
Naturally Occurring ◽  
Apoptosis Pathways ◽  
Present Understanding

In efforts to identify naturally occurring compounds that act as protective agents, resveratrol, a phytoalexin existing in wine, has attracted much interest because of its diverse pharmacological characteristics. Considering that apoptosis induction is the most potent defense approach for cancer treatment, we have tried to summarize our present understanding of apoptosis induction by resveratrol based on the two major apoptosis pathways.

High throughput phenotype screening pipeline for functional genomics in Magnaporthe oryzae

2007 ◽  
Author(s):  
Sook-Young Park ◽  
Myoung-Hwan Chi ◽  
Junhyun Jeon ◽  
Yong-Hwan Lee
Keyword(s):  
Functional Genomics ◽  
High Throughput ◽  
Magnaporthe Oryzae ◽  
Phenotype Screening
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