Structure based function-annotation of hypothetical protein MGG_01005 from Magnaporthe oryzae reveals it is the dynein light chain orthologue of dynlt1/3

Abstract

Magnaporthe oryzae is a model fungal plant pathogen employed for studying plant-fungi interactions. Whole genome sequencing and bioinformatics analyses revealed that this fungal pathogen has more than 12,000 protein-coding genes with 65% of the genes remaining functionally un-annotated. Here, we determine the structure of the hypothetical protein, MGG_01005 and show that it is the Magnaporthe oryzae Dynein light chain Tctex-type 1 (dynlt1/3), demonstrated by its structural similarity to other orthologous dynlt1 proteins and its conserved interaction with the N-terminus of the Magnaporthe oryzae dynein intermediate chain, MoDyn1I2. In addition, we present the structure of the MGG_01005-MoDyn1I2 complex together with mutagenesis studies that reveals a di-histidine motif interaction with a glutamate residue in the dynein intermediate chain within a conserved molecular interface. These results demonstrate the utility of structure-based annotation and validate it as a viable approach for the molecular assignment of hypothetic proteins from phyto-pathogenic fungi.

RNA profiling of laser microdissected human trophoblast subtypes at mid-gestation reveals a role for cannabinoid signaling in invasion

“…Immunolocalization revealed a cytoplasmic staining pattern ( Fig. 5 D-F) that was consistent with the function of its fungal protein analog, dynein light chain, which is involved in intracellular transport ( Li et al, 2018 ). We also showed that invasive CTBs express CNR1.…”

“…High placental levels of this mRNA (ENSG00000163633) have been reported ( Fagerberg et al, 2014 ). Its fungal protein analog (MGG_01005) is dynein light chain Tctex-type 1 (dynlt1/3; Li et al, 2018 ), which transports various types of cellular cargo. CYP19A1 (aromatase) and GH2 (growth hormone 2) were also expressed at higher levels in the syncytium.…”

Force-Generating Mechanism of Axonemal Dynein in Solo and Ensemble

“…Therefore, it is unclear as yet which, if any, of these mechanisms regulates the beating of the axoneme. As indicated in Figure 5c, specific dynein subsets are perhaps activated during travel of the bend [116]. However, these models do not assign any particular conformational states to dyneins within straight or curved regions.…”

Functional domain annotation by structural similarity

“…Therefore, we expect to annotate more proteins if we use protein structure in the annotation process. Some studies have successfully used protein structures to annotate the domains of protein that couldn’t be annotated by sequence alone (Bartas et al, 2022; Li et al, 2018; Zarembinski et al, 1998). However, these approaches have not been widely adopted because it is difficult to experimentally determine the structure of a protein with an unknown function.…”