pH and alcohol induced structural transition in Ntf2 a nuclear transport factor of Saccharomyces cerevisiae

2020 ◽  
Vol 159 ◽  
pp. 79-86
Author(s):  
Mohd. Kashif ◽  
Akhilendra Pratap Bharati ◽  
Sumit Kumar Chaturvedi ◽  
Rizwan Hasan Khan ◽  
Abrar Ahmad ◽  
...  
Bionatura ◽  
2020 ◽  
Vol 5 (4) ◽  
pp. 1423-1426
Author(s):  
Bruna Rech ◽  
Fernando A. Gonzales-Zubiate

Ribonucleases (RNases) functions in the cell include precise maturation of non- coding RNAs and degradation of specific RNA transcripts that are no longer necessary. RNAses are present in the cell as single units or assembled as multimeric complexes; one of these complexes is the RNA exosome, a highly conserved complex essential for RNA processing and degradation. In the yeast Saccharomyces cerevisiae, the RNA exosome comprises eleven subunits, two with catalytic activity: Rrp6 and Rrp44, where the Rrp6 subunit is exclusively nuclear. Despite the RNA exosome has been intensively investigated since its discovery in 1997, only a few studies were accomplished concerning its nuclear transport. This review describes recent research about cellular localization and transport of this essential complex.


2019 ◽  
Author(s):  
Karine de Guillen ◽  
Cécile Lorrain ◽  
Pascale Tsan ◽  
Philippe Barthe ◽  
Benjamin Petre ◽  
...  

ABSTRACTRust fungi are plant pathogens that secrete an arsenal of effector proteins interfering with plant functions and promoting parasitic infection. Effectors are often species-specific, evolve rapidly, and display low sequence similarities with known proteins or domains. How rust fungal effectors function in host cells remains elusive, and biochemical and structural approaches have been scarcely used to tackle this question. In this study, we used a strategy based on recombinant protein production in Escherichia coli to study eleven candidate effectors of the leaf rust fungus Melampsora larici-populina. We successfully purified and solved the three-dimensional structure of two proteins, MLP124266 and MLP124017, using NMR spectroscopy. Although both proteins show no sequence similarity with known proteins, they exhibit structural similarities to knottin and nuclear transport factor 2-like proteins, respectively. Altogether, our findings show that sequence-unrelated effectors can adopt folds similar to known proteins, and encourage the use of biochemical and structural approaches to functionally characterize rust effector candidates.


1998 ◽  
Vol 95 (2) ◽  
pp. 582-587 ◽  
Author(s):  
M. V. Nachury ◽  
U. W. Ryder ◽  
A. I. Lamond ◽  
K. Weis

Cell ◽  
1997 ◽  
Vol 90 (6) ◽  
pp. 1061-1071 ◽  
Author(s):  
Ulrike Kutay ◽  
F.Ralf Bischoff ◽  
Susanne Kostka ◽  
Regine Kraft ◽  
Dirk Görlich

1996 ◽  
Vol 7 (12) ◽  
pp. 1921-1937 ◽  
Author(s):  
R Murphy ◽  
J L Watkins ◽  
S R Wente

To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin Nup100p were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srp1p, the nuclear localization signal receptor, as well as Rip1p, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.


2013 ◽  
Vol 22 (5) ◽  
pp. 587-593 ◽  
Author(s):  
Alex R Paciorkowski ◽  
Judy Weisenberg ◽  
Joshua B Kelley ◽  
Adam Spencer ◽  
Emily Tuttle ◽  
...  

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