The Nuclear Transport Factor CSE1 Drives Macronuclear Volume Increase and Macronuclear Node Condensation In Stentor Coeruleus

2021 ◽  
Author(s):  
Rebecca McGillivary ◽  
Pranidhi Sood ◽  
Katherine Hammar ◽  
Wallace F. Marshall
Keyword(s):  
Nuclear Transport ◽  
Volume Increase ◽  
Transport Factor ◽  
Stentor Coeruleus

scholarly journals The nuclear transport factor CSE1 drives macronuclear volume increase and macronuclear node condensation in Stentor coeruleus

2021 ◽  
Author(s):  
Rebecca M McGillivary ◽  
Pranidhi Sood ◽  
Katharine Hammar ◽  
Wallace F Marshall
Keyword(s):  
Cell Division ◽  
Molecular Mechanisms ◽  
Nuclear Transport ◽  
Shape Change ◽  
Developmentally Regulated ◽  
Volume Increase ◽  
Transport Factor ◽  
Single Mass ◽  
Stentor Coeruleus ◽  
The 1960S

The giant ciliate, Stentor coeruleus, provides a unique opportunity to study nuclear shape because its macronucleus undergoes a rapid, dramatic, and developmentally regulated shape change. During a 2 hour time period within cell division and regeneration, the 400 um long moniliform macronucleus condenses into a single mass, elongates into a vermiform shape, and then renodulates, returning to its original beads-on-a-string morphology (Tartar 1961). Previous work from the 1960s - 1980s demonstrated that the macronuclear shape change is a highly regulated part of cell division and regeneration, but there were no molecular studies into this process (De Terra 1964; De Terra 1983). With the recent availability of a sequenced Stentor genome, a transcriptome during regeneration, and molecular tools like RNAi, it is now possible to investigate the molecular mechanisms that drive macronuclear shape change (Slabodnick et al. 2014; Slabodnick et al. 2017; Sood et al. 2021). We found that the volume of the macronucleus increases during condensation. When the nuclear transport factor, CSE1, is knocked down by RNAi, this volume increase is reduced, and the nodes are unable to fuse. This affects the final morphology of the macronucleus: 24 hours after regeneration the macronucleus is misshapen. We found that CSE1 is mainly cytoplasmic during interphase and in early regeneration, and then becomes mainly macronuclear during condensation. At the end of regeneration CSE1 is degraded while the macronucleus returns to its pre-condensation volume. We propose a model in which nuclear transport via CSE1 increases the volume of the macronucleus, driving the condensation of the many nodes into a single mass.

scholarly journals Structural genomic applied on the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine-knot and nuclear transport factor 2-like protein folds

2019 ◽  
Author(s):  
Karine de Guillen ◽  
Cécile Lorrain ◽  
Pascale Tsan ◽  
Philippe Barthe ◽  
Benjamin Petre ◽  
...  
Keyword(s):  
Plant Pathogens ◽  
Nuclear Transport ◽  
Sequence Similarity ◽  
Rust Fungus ◽  
Parasitic Infection ◽  
Effector Proteins ◽  
Host Cells ◽  
Dimensional Structure ◽  
Structural Genomic ◽  
Transport Factor

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.

scholarly journals Cloning and characterization of hSRP1 , a tissue-specific nuclear transport factor

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

scholarly journals Export of Importin α from the Nucleus Is Mediated by a Specific Nuclear Transport Factor

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

scholarly journals Autosomal recessive mutations in nuclear transport factor KPNA7 are associated with infantile spasms and cerebellar malformation

2013 ◽  
Vol 22 (5) ◽  
pp. 587-593 ◽  
Author(s):  
Alex R Paciorkowski ◽  
Judy Weisenberg ◽  
Joshua B Kelley ◽  
Adam Spencer ◽  
Emily Tuttle ◽  
...  
Keyword(s):  
Autosomal Recessive ◽  
Nuclear Transport ◽  
Infantile Spasms ◽  
Cerebellar Malformation ◽  
Recessive Mutations ◽  
Transport Factor

scholarly journals Nuclear transport factor directs localization of protein synthesis during mitosis

2009 ◽  
Vol 11 (3) ◽  
pp. 350-356 ◽  
Author(s):  
Geert van den Bogaart ◽  
Anne C. Meinema ◽  
Victor Krasnikov ◽  
Liesbeth M. Veenhoff ◽  
Bert Poolman
Keyword(s):  
Protein Synthesis ◽  
Nuclear Transport ◽  
Transport Factor

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 ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Structural Transition ◽  
Nuclear Transport ◽  
Transport Factor

Crystallization and Preliminary X-Ray Diffraction Analysis of Nuclear Transport Factor 2

1996 ◽  
Vol 116 (2) ◽  
pp. 326-329 ◽  
Author(s):  
Helen M. Kent ◽  
W.David Clarkson ◽  
Timothy L. Bullock ◽  
Murray Stewart
Keyword(s):  
Diffraction Analysis ◽  
Nuclear Transport ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transport Factor
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