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Article ; Online: Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.

Snider, Chloe E / Chandra, Mintu / McDonald, Nathan A / Willet, Alaina H / Collier, Scott E / Ohi, Melanie D / Jackson, Lauren P / Gould, Kathleen L

Cell reports

2020 Volume 33, Issue 12, Page(s) 108526

Abstract: Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain ...

Abstract	Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.
MeSH term(s)	Cell Cycle Proteins/metabolism ; Cytokinesis/genetics ; Cytoskeleton/metabolism ; GTP-Binding Proteins/metabolism ; Humans ; Schizosaccharomyces ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	CDC15 protein ; Cell Cycle Proteins ; Schizosaccharomyces pombe Proteins ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2020-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.108526
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Biased Brownian motion as a mechanism to facilitate nanometer-scale exploration of the microtubule plus end by a kinesin-8.

Shin, Yongdae / Du, Yaqing / Collier, Scott E / Ohi, Melanie D / Lang, Matthew J / Ohi, Ryoma

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 29, Page(s) E3826–35

Abstract: Kinesin-8s are plus-end-directed motors that negatively regulate microtubule (MT) length. Well-characterized members of this subfamily (Kip3, Kif18A) exhibit two important properties: (i) They are "ultraprocessive," a feature enabled by a second MT- ... ...

Abstract	Kinesin-8s are plus-end-directed motors that negatively regulate microtubule (MT) length. Well-characterized members of this subfamily (Kip3, Kif18A) exhibit two important properties: (i) They are "ultraprocessive," a feature enabled by a second MT-binding site that tethers the motors to a MT track, and (ii) they dissociate infrequently from the plus end. Together, these characteristics combined with their plus-end motility cause Kip3 and Kif18A to enrich preferentially at the plus ends of long MTs, promoting MT catastrophes or pausing. Kif18B, an understudied human kinesin-8, also limits MT growth during mitosis. In contrast to Kif18A and Kip3, localization of Kif18B to plus ends relies on binding to the plus-end tracking protein EB1, making the relationship between its potential plus-end-directed motility and plus-end accumulation unclear. Using single-molecule assays, we show that Kif18B is only modestly processive and that the motor switches frequently between directed and diffusive modes of motility. Diffusion is promoted by the tail domain, which also contains a second MT-binding site that decreases the off rate of the motor from the MT lattice. In cells, Kif18B concentrates at the extreme tip of a subset of MTs, superseding EB1. Our data demonstrate that kinesin-8 motors use diverse design principles to target MT plus ends, which likely target them to the plus ends of distinct MT subpopulations in the mitotic spindle.
MeSH term(s)	Biophysical Phenomena ; Cell Tracking ; Diffusion ; HeLa Cells ; Humans ; Kinesin/chemistry ; Kinesin/metabolism ; Kinetics ; Microtubules/metabolism ; Motion ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Tertiary ; Video Recording
Chemical Substances	Mutant Proteins ; KIF18B protein, human (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2015-07-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1500272112
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Article ; Online: Fission yeast Dma1 requires RING domain dimerization for its ubiquitin ligase activity and mitotic checkpoint function.

Johnson, Alyssa E / Collier, Scott E / Ohi, Melanie D / Gould, Kathleen L

The Journal of biological chemistry

2012 Volume 287, Issue 31, Page(s) 25741–25748

Abstract: In fission yeast (Schizosaccharomyces pombe), the E3 ubiquitin ligase Dma1 delays cytokinesis if chromosomes are not properly attached to the mitotic spindle. Dma1 contains a C-terminal RING domain, and we have found that the Dma1 RING domain forms a ... ...

Abstract	In fission yeast (Schizosaccharomyces pombe), the E3 ubiquitin ligase Dma1 delays cytokinesis if chromosomes are not properly attached to the mitotic spindle. Dma1 contains a C-terminal RING domain, and we have found that the Dma1 RING domain forms a stable homodimer. Although the RING domain is required for dimerization, residues in the C-terminal tail are also required to help form or stabilize the dimeric structure because mutation of specific residues in this region disrupts Dma1 dimerization. Further analyses showed that Dma1 dimerization is required for proper localization at spindle pole bodies and the cell division site, E3 ligase activity, and mitotic checkpoint function. Thus, Dma1 forms an obligate dimer via its RING domain, which is essential for efficient transfer of ubiquitin to its substrate(s). This study further supports the mechanistic paradigm that many RING E3 ligases function as RING dimers.
MeSH term(s)	Amino Acid Sequence ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Conserved Sequence ; M Phase Cell Cycle Checkpoints ; Mitosis ; Molecular Sequence Data ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Transport ; RING Finger Domains ; Schizosaccharomyces/enzymology ; Schizosaccharomyces/physiology ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Sequence Homology, Amino Acid ; Spindle Apparatus/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Cell Cycle Proteins ; Dma1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2012-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112.349712
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Article ; Online: Gle1 functions during mRNA export in an oligomeric complex that is altered in human disease.

Folkmann, Andrew W / Collier, Scott E / Zhan, Xiaoyan / Aditi / Ohi, Melanie D / Wente, Susan R

Cell

2013 Volume 155, Issue 3, Page(s) 582–593

Abstract: The conserved multifunctional protein Gle1 regulates gene expression at multiple steps: nuclear mRNA export, translation initiation, and translation termination. A GLE1 mutation (FinMajor) is causally linked to human lethal congenital contracture ... ...

Abstract	The conserved multifunctional protein Gle1 regulates gene expression at multiple steps: nuclear mRNA export, translation initiation, and translation termination. A GLE1 mutation (FinMajor) is causally linked to human lethal congenital contracture syndrome-1 (LCCS1); however, the resulting perturbations on Gle1 molecular function were unknown. FinMajor results in a proline-phenylalanine-glutamine peptide insertion within the uncharacterized Gle1 coiled-coil domain. Here, we find that Gle1 self-associates both in vitro and in living cells via the coiled-coil domain. Electron microscopy reveals that high-molecular-mass Gle1 oligomers form ?26 nm diameter disk-shaped particles. With the Gle1-FinMajor protein, these particles are malformed. Moreover, functional assays document a specific requirement for proper Gle1 oligomerization during mRNA export, but not for Gle1's roles in translation. These results identify a mechanistic step in Gle1's mRNA export function at nuclear pore complexes and directly implicate altered export in LCCS1 disease pathology.
MeSH term(s)	Active Transport, Cell Nucleus ; Arthrogryposis/genetics ; Arthrogryposis/metabolism ; Arthrogryposis/pathology ; HeLa Cells ; Humans ; Mutation ; Nuclear Pore/metabolism ; Nucleocytoplasmic Transport Proteins/metabolism ; RNA, Messenger/metabolism ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Gle1 protein, human ; Nucleocytoplasmic Transport Proteins ; RNA, Messenger
Language	English
Publishing date	2013-10-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2013.09.023
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Zs.A 1167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Structural and functional characterization of the N terminus of Schizosaccharomyces pombe Cwf10.

Livesay, S Brent / Collier, Scott E / Bitton, Danny A / Bähler, Jürg / Ohi, Melanie D

Eukaryotic cell

2013 Volume 12, Issue 11, Page(s) 1472–1489

Abstract: The spliceosome is a dynamic macromolecular machine that catalyzes the removal of introns from pre-mRNA, yielding mature message. Schizosaccharomyces pombe Cwf10 (homolog of Saccharomyces cerevisiae Snu114 and human U5-116K), an integral member of the U5 ...

Abstract	The spliceosome is a dynamic macromolecular machine that catalyzes the removal of introns from pre-mRNA, yielding mature message. Schizosaccharomyces pombe Cwf10 (homolog of Saccharomyces cerevisiae Snu114 and human U5-116K), an integral member of the U5 snRNP, is a GTPase that has multiple roles within the splicing cycle. Cwf10/Snu114 family members are highly homologous to eukaryotic translation elongation factor EF2, and they contain a conserved N-terminal extension (NTE) to the EF2-like portion, predicted to be an intrinsically unfolded domain. Using S. pombe as a model system, we show that the NTE is not essential, but cells lacking this domain are defective in pre-mRNA splicing. Genetic interactions between cwf10-ΔNTE and other pre-mRNA splicing mutants are consistent with a role for the NTE in spliceosome activation and second-step catalysis. Characterization of Cwf10-NTE by various biophysical techniques shows that in solution the NTE contains regions of both structure and disorder. The first 23 highly conserved amino acids of the NTE are essential for its role in splicing but when overexpressed are not sufficient to restore pre-mRNA splicing to wild-type levels in cwf10-ΔNTE cells. When the entire NTE is overexpressed in the cwf10-ΔNTE background, it can complement the truncated Cwf10 protein in trans, and it immunoprecipitates a complex similar in composition to the late-stage U5.U2/U6 spliceosome. These data show that the structurally flexible NTE is capable of independently incorporating into the spliceosome and improving splicing function, possibly indicating a role for the NTE in stabilizing conformational rearrangements during a splice cycle.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Structure, Tertiary ; RNA Splicing ; Ribonucleoprotein, U5 Small Nuclear/chemistry ; Ribonucleoprotein, U5 Small Nuclear/genetics ; Ribonucleoprotein, U5 Small Nuclear/metabolism ; Schizosaccharomyces/chemistry ; Schizosaccharomyces/enzymology ; Schizosaccharomyces/genetics ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Spliceosomes/metabolism
Chemical Substances	Ribonucleoprotein, U5 Small Nuclear ; Schizosaccharomyces pombe Proteins ; Cwf10 protein, S pombe (EC 3.6.1.-) ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2013-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2077635-4
ISSN	1535-9786 ; 1535-9778
ISSN (online)	1535-9786
ISSN	1535-9778
DOI	10.1128/EC.00140-13
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Zs.A 5779: Show issues

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Article: Structural and Functional Insights into the N-Terminus of Schizosaccharomyces pombe Cdc5

Collier, Scott E / Voehler Markus / Peng Dungeng / Ohi Ryoma / Gould Kathleen L / Reiter Nicholas J / Ohi Melanie D

Biochemistry. 2014 Oct. 21, v. 53, no. 41

2014

Abstract: The spliceosome is a dynamic macromolecular machine composed of five small nuclear ribonucleoparticles (snRNPs), the NineTeen Complex (NTC), and other proteins that catalyze the removal of introns mature to form the mature message. The NTC, named after ... ...

Abstract	The spliceosome is a dynamic macromolecular machine composed of five small nuclear ribonucleoparticles (snRNPs), the NineTeen Complex (NTC), and other proteins that catalyze the removal of introns mature to form the mature message. The NTC, named after its founding member Saccharomyces cerevisiae Prp19, is a conserved spliceosome subcomplex composed of at least nine proteins. During spliceosome assembly, the transition to an active spliceosome correlates with stable binding of the NTC, although the mechanism of NTC function is not understood. Schizosaccharomyces pombe Cdc5, a core subunit of the NTC, is an essential protein required for pre-mRNA splicing. The highly conserved Cdc5 N-terminus contains two canonical Myb (myeloblastosis) repeats (R1 and R2) and a third domain (D3) that was previously classified as a Myb-like repeat. Although the N-terminus of Cdc5 is required for its function, how R1, R2, and D3 each contribute to functionality is unclear. Using a combination of yeast genetics, structural approaches, and RNA binding assays, we show that R1, R2, and D3 are all required for the function of Cdc5 in cells. We also show that the N-terminus of Cdc5 binds RNA in vitro. Structural and functional analyses of Cdc5-D3 show that, while this domain does not adopt a Myb fold, Cdc5-D3 preferentially binds double-stranded RNA. Our data suggest that the Cdc5 N-terminus interacts with RNA structures proposed to be near the catalytic core of the spliceosome.
Keywords	Saccharomyces cerevisiae ; Schizosaccharomyces pombe ; double-stranded RNA ; introns ; microbial genetics ; proteins ; spliceosomes
Language	English
Dates of publication	2014-1021
Size	p. 6439-6451.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Fbi5008639
Database	NAL-Catalogue (AGRICOLA)

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Article: Bicelles Rich in both Sphingolipids and Cholesterol and Their Use in Studies of Membrane Proteins

Journal of the American Chemical Society. 2020 June 23, v. 142, no. 29

2020

Abstract: How the distinctive lipid composition of mammalian plasma membranes impacts membrane protein structure is largely unexplored, partly because of the dearth of isotropic model membrane systems that contain abundant sphingolipids and cholesterol. This gap ... ...

Abstract	How the distinctive lipid composition of mammalian plasma membranes impacts membrane protein structure is largely unexplored, partly because of the dearth of isotropic model membrane systems that contain abundant sphingolipids and cholesterol. This gap is addressed by showing that sphingomyelin and cholesterol-rich (SCOR) lipid mixtures with phosphatidylcholine can be cosolubilized by n-dodecyl-β-melibioside to form bicelles. Small-angle X-ray and neutron scattering, as well as cryo-electron microscopy, demonstrate that these assemblies are stable over a wide range of conditions and exhibit the bilayered-disc morphology of ideal bicelles even at low lipid-to-detergent mole ratios. SCOR bicelles are shown to be compatible with a wide array of experimental techniques, as applied to the transmembrane human amyloid precursor C99 protein in this medium. These studies reveal an equilibrium between low-order oligomer structures that differ significantly from previous experimental structures of C99, providing an example of how ordered membranes alter membrane protein structure.
Keywords	amyloid ; cholesterol ; cryo-electron microscopy ; humans ; isotropy ; lipid composition ; membrane proteins ; neutrons ; phosphatidylcholines ; protein structure ; small-angle X-ray scattering ; sphingomyelins
Language	English
Dates of publication	2020-0623
Size	p. 12715-12729.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.0c04669
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Article ; Online: Bicelles Rich in both Sphingolipids and Cholesterol and Their Use in Studies of Membrane Proteins.

Journal of the American Chemical Society

2020 Volume 142, Issue 29, Page(s) 12715–12729

Abstract	How the distinctive lipid composition of mammalian plasma membranes impacts membrane protein structure is largely unexplored, partly because of the dearth of isotropic model membrane systems that contain abundant sphingolipids and cholesterol. This gap is addressed by showing that
MeSH term(s)	Cholesterol/chemistry ; Cryoelectron Microscopy ; Humans ; Membrane Proteins/chemistry ; Sphingolipids/chemistry
Chemical Substances	Membrane Proteins ; Sphingolipids ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2020-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.0c04669
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Article ; Online: Structural and functional insights into the N-terminus of Schizosaccharomyces pombe Cdc5.

Collier, Scott E / Voehler, Markus / Peng, Dungeng / Ohi, Ryoma / Gould, Kathleen L / Reiter, Nicholas J / Ohi, Melanie D

Biochemistry

2014 Volume 53, Issue 41, Page(s) 6439–6451

Abstract	The spliceosome is a dynamic macromolecular machine composed of five small nuclear ribonucleoparticles (snRNPs), the NineTeen Complex (NTC), and other proteins that catalyze the removal of introns mature to form the mature message. The NTC, named after its founding member Saccharomyces cerevisiae Prp19, is a conserved spliceosome subcomplex composed of at least nine proteins. During spliceosome assembly, the transition to an active spliceosome correlates with stable binding of the NTC, although the mechanism of NTC function is not understood. Schizosaccharomyces pombe Cdc5, a core subunit of the NTC, is an essential protein required for pre-mRNA splicing. The highly conserved Cdc5 N-terminus contains two canonical Myb (myeloblastosis) repeats (R1 and R2) and a third domain (D3) that was previously classified as a Myb-like repeat. Although the N-terminus of Cdc5 is required for its function, how R1, R2, and D3 each contribute to functionality is unclear. Using a combination of yeast genetics, structural approaches, and RNA binding assays, we show that R1, R2, and D3 are all required for the function of Cdc5 in cells. We also show that the N-terminus of Cdc5 binds RNA in vitro. Structural and functional analyses of Cdc5-D3 show that, while this domain does not adopt a Myb fold, Cdc5-D3 preferentially binds double-stranded RNA. Our data suggest that the Cdc5 N-terminus interacts with RNA structures proposed to be near the catalytic core of the spliceosome.
MeSH term(s)	Binding Sites ; Catalytic Domain ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Gene Deletion ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Conformation ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Stability ; RNA Splicing ; RNA, Double-Stranded/metabolism ; RNA, Fungal/chemistry ; RNA, Fungal/metabolism ; RNA, Small Nuclear/chemistry ; RNA, Small Nuclear/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Spliceosomes/chemistry ; Spliceosomes/genetics ; Spliceosomes/metabolism ; Titrimetry
Chemical Substances	Cell Cycle Proteins ; Mutant Proteins ; Peptide Fragments ; RNA, Double-Stranded ; RNA, Fungal ; RNA, Small Nuclear ; RNA-Binding Proteins ; Recombinant Proteins ; Schizosaccharomyces pombe Proteins ; cdc5 protein, S pombe
Language	English
Publishing date	2014-10-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi5008639
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Article ; Online: Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, bind Tudor and protect from transposable elements.

Gao, Ming / Thomson, Travis C / Creed, T Michael / Tu, Shikui / Loganathan, Sudan N / Jackson, Christina A / McCluskey, Patrick / Lin, Yanyan / Collier, Scott E / Weng, Zhiping / Lasko, Paul / Ohi, Melanie D / Arkov, Alexey L

EMBO reports

2015 Volume 16, Issue 3, Page(s) 379–386

Abstract: Germ cells give rise to all cell lineages in the next-generation and are responsible for the continuity of life. In a variety of organisms, germ cells and stem cells contain large ribonucleoprotein granules. Although these particles were discovered more ... ...

Abstract	Germ cells give rise to all cell lineages in the next-generation and are responsible for the continuity of life. In a variety of organisms, germ cells and stem cells contain large ribonucleoprotein granules. Although these particles were discovered more than 100 years ago, their assembly and functions are not well understood. Here we report that glycolytic enzymes are components of these granules in Drosophila germ cells and both their mRNAs and the enzymes themselves are enriched in germ cells. We show that these enzymes are specifically required for germ cell development and that they protect their genomes from transposable elements, providing the first link between metabolism and transposon silencing. We further demonstrate that in the granules, glycolytic enzymes associate with the evolutionarily conserved Tudor protein. Our biochemical and single-particle EM structural analyses of purified Tudor show a flexible molecule and suggest a mechanism for the recruitment of glycolytic enzymes to the granules. Our data indicate that germ cells, similarly to stem cells and tumor cells, might prefer to produce energy through the glycolytic pathway, thus linking a particular metabolism to pluripotency.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Base Sequence ; Cytoplasmic Granules/metabolism ; DNA Transposable Elements/physiology ; Drosophila/enzymology ; Drosophila/physiology ; Drosophila Proteins/metabolism ; Germ Cells/physiology ; Glycolysis ; Membrane Transport Proteins/metabolism ; MicroRNAs/genetics ; Molecular Sequence Data ; Ribonucleoproteins/metabolism ; Sequence Analysis, DNA
Chemical Substances	DNA Transposable Elements ; Drosophila Proteins ; Membrane Transport Proteins ; MicroRNAs ; Ribonucleoproteins ; tud protein, Drosophila
Language	English
Publishing date	2015-01-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201439694
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