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Artikel ; Online: Pairing of homologous chromosomes in C. elegans meiosis requires DEB-1 - an orthologue of mammalian vinculin.

Rohožková, Jana / Hůlková, Lenka / Fukalová, Jana / Flachs, Petr / Hozák, Pavel

2019 Band 10, Heft 1, Seite(n) 93–115

Abstract: During meiosis, homologous chromosomes undergo a dramatic movement in order to correctly align. This is a critical meiotic event but the molecular properties of this 'chromosomal dance' still remainunclear. We identified DEB-1 - an orthologue of ... ...

Abstract	During meiosis, homologous chromosomes undergo a dramatic movement in order to correctly align. This is a critical meiotic event but the molecular properties of this 'chromosomal dance' still remainunclear. We identified DEB-1 - an orthologue of mammalian vinculin - as a new component of the mechanistic modules responsible for attaching the chromosomes to the nuclear envelope as apart of the LINC complex. In early meiotic nuclei of C. elegans, DEB-1 is localized to the nuclear periphery and alongside the synaptonemal complex of paired homologues. Upon DEB-1 depletion, chromosomes attached to SUN-1 foci remain highly motile until late pachytene. Although the initiation of homologue pairing started normally, irregularities in the formation of the synaptonemal complex occur, and these results in meiotic defects such as increased number of univalents at diakinesis and high embryonic lethality. Our data identify DEB-1 as a new player regulating chromosome dynamics and pairing during meiotic prophase I.
Mesh-Begriff(e)	Animals ; Caenorhabditis elegans/genetics ; Chromosome Pairing/genetics ; Chromosomes/genetics ; Meiosis/genetics ; Vinculin/genetics
Chemische Substanzen	Vinculin (125361-02-6)
Sprache	Englisch
Erscheinungsdatum	2019-05-05
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2019.1602337
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Pairing of homologous chromosomes in C. elegans meiosis requires DEB-1 - an orthologue of mammalian vinculin

Rohožková, Jana / Hůlková, Lenka / Fukalová, Jana / Flachs, Petr / Hozák, Pavel

Nucleus. 2019 Jan. 1, v. 10, no. 1

2019

Abstract: During meiosis, homologous chromosomes undergo a dramatic movement in order to correctly align. This is a critical meiotic event but the molecular properties of this ‘chromosomal dance’ still remainunclear. We identified DEB-1 – an orthologue of ... ...

Abstract	During meiosis, homologous chromosomes undergo a dramatic movement in order to correctly align. This is a critical meiotic event but the molecular properties of this ‘chromosomal dance’ still remainunclear. We identified DEB-1 – an orthologue of mammalian vinculin – as a new component of the mechanistic modules responsible for attaching the chromosomes to the nuclear envelope as apart of the LINC complex. In early meiotic nuclei of C. elegans, DEB-1 is localized to the nuclear periphery and alongside the synaptonemal complex of paired homologues. Upon DEB-1 depletion, chromosomes attached to SUN-1 foci remain highly motile until late pachytene. Although the initiation of homologue pairing started normally, irregularities in the formation of the synaptonemal complex occur, and these results in meiotic defects such as increased number of univalents at diakinesis and high embryonic lethality. Our data identify DEB-1 as a new player regulating chromosome dynamics and pairing during meiotic prophase I.
Schlagwörter	chromosomes ; embryonic mortality ; mammals ; nuclear membrane ; pachytene stage ; synaptonemal complex
Sprache	Englisch
Erscheinungsverlauf	2019-0101
Umfang	p. 93-115.
Erscheinungsort	Taylor & Francis
Dokumenttyp	Artikel
Anmerkung	NAL-AP-2-clean
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2019.1602337
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel ; Online: Multiple Aspects of PIP2 Involvement in

Ulicna, Livia / Rohozkova, Jana / Hozak, Pavel

International journal of molecular sciences

2018 Band 19, Heft 9

Abstract: One of the most studied phosphoinositides is phosphatidylinositol 4,5-bisphosphate (PIP2), which localizes to the plasma membrane, nuclear speckles, small foci in the nucleoplasm, and to the nucleolus in mammalian cells. Here, we show that PIP2 also ... ...

Abstract	One of the most studied phosphoinositides is phosphatidylinositol 4,5-bisphosphate (PIP2), which localizes to the plasma membrane, nuclear speckles, small foci in the nucleoplasm, and to the nucleolus in mammalian cells. Here, we show that PIP2 also localizes to the nucleus in prophase I, during the gametogenesis of
Mesh-Begriff(e)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Cell Nucleus/metabolism ; Chromosomes/chemistry ; Gametogenesis ; Gene Expression Regulation, Developmental ; Hermaphroditic Organisms/genetics ; Hermaphroditic Organisms/growth & development ; Hermaphroditic Organisms/metabolism ; Meiotic Prophase I ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/genetics ; Proteasome Endopeptidase Complex/metabolism ; Proteins/metabolism ; RNA Interference
Chemische Substanzen	Caenorhabditis elegans Proteins ; Phosphatidylinositol 4,5-Diphosphate ; Proteins ; leucine-rich repeat proteins ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; Ppk-1 protein, C elegans (EC 2.7.1.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Sprache	Englisch
Erscheinungsdatum	2018-09-10
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms19092679
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: P1 peptidase--a mysterious protein of family Potyviridae.

Rohozková, Jana / Navrátil, Milan

Journal of biosciences

2011 Band 36, Heft 1, Seite(n) 189–200

Abstract: The Potyviridae family, named after its type member, Potato virus Y (PVY), is the largest of the 65 plant virus groups and families currently recognized. The coding region for P1 peptidase is located at the very beginning of the viral genome of the ... ...

Abstract	The Potyviridae family, named after its type member, Potato virus Y (PVY), is the largest of the 65 plant virus groups and families currently recognized. The coding region for P1 peptidase is located at the very beginning of the viral genome of the family Potyviridae. Until recently P1 was thought of as serine peptidase with RNA-binding activity and with possible influence in cell-to-cell viral spreading. This N-terminal protein, among all of the potyviruses, is the most divergent protein: varying in length and in its amino acid sequence. Nevertheless, P1 peptidase in many ways is still a mysterious viral protein. In this review, we would like to offer a comprehensive overview, discussing the proteomic, biochemical and phylogenetic views of the P1 protein.
Mesh-Begriff(e)	Evolution, Molecular ; Genetic Variation ; Phylogeny ; Potyviridae/genetics ; Potyviridae/metabolism ; RNA-Binding Proteins/genetics ; Serine Endopeptidases/genetics ; Species Specificity ; Viral Proteins/genetics ; Viral Proteins/physiology
Chemische Substanzen	P1 protein, potyvirus ; RNA-Binding Proteins ; Viral Proteins ; Serine Endopeptidases (EC 3.4.21.-)
Sprache	Englisch
Erscheinungsdatum	2011-03-30
Erscheinungsland	India
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	756157-x
ISSN	0973-7138 ; 0250-5991
ISSN (online)	0973-7138
ISSN	0250-5991
DOI	10.1007/s12038-011-9020-6
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: P1 peptidase – a mysterious protein of family Potyviridae

Rohožková, Jana / Navrátil, Milan

Journal of biosciences.. 2011 Mar., v. 36, no. 1

2011

Abstract	The Potyviridae family, named after its type member, Potato virus Y (PVY), is the largest of the 65 plant virus groups and families currently recognized. The coding region for P1 peptidase is located at the very beginning of the viral genome of the family Potyviridae. Until recently P1 was thought of as serine peptidase with RNA-binding activity and with possible influence in cell-to-cell viral spreading. This N-terminal protein, among all of the potyviruses, is the most divergent protein: varying in length and in its amino acid sequence. Nevertheless, P1 peptidase in many ways is still a mysterious viral protein. In this review, we would like to offer a comprehensive overview, discussing the proteomic, biochemical and phylogenetic views of the P1 protein.
Schlagwörter	Potato virus Y ; amino acid sequences ; genome ; phylogeny ; proteomics ; serine ; viruses
Sprache	Englisch
Erscheinungsverlauf	2011-03
Umfang	p. 189-200.
Erscheinungsort	Springer-Verlag
Dokumenttyp	Artikel
ZDB-ID	756157-x
ISSN	0973-7138 ; 0250-5991
ISSN (online)	0973-7138
ISSN	0250-5991
DOI	10.1007/s12038-011-9020-6
Datenquelle	NAL Katalog (AGRICOLA)

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Artikel ; Online: Multiple Aspects of PIP2 Involvement in C. elegans Gametogenesis

Livia Ulicna / Jana Rohozkova / Pavel Hozak

International Journal of Molecular Sciences, Vol 19, Iss 9, p

2018 Band 2679

Abstract	One of the most studied phosphoinositides is phosphatidylinositol 4,5-bisphosphate (PIP2), which localizes to the plasma membrane, nuclear speckles, small foci in the nucleoplasm, and to the nucleolus in mammalian cells. Here, we show that PIP2 also localizes to the nucleus in prophase I, during the gametogenesis of C. elegans hermaphrodite. The depletion of PIP2 by type I PIP kinase (PPK-1) kinase RNA interference results in an altered chromosome structure and leads to various defects during meiotic progression. We observed a decreased brood size and aneuploidy in progeny, defects in synapsis, and crossover formation. The altered chromosome structure is reflected in the increased transcription activity of a tightly regulated process in prophase I. To elucidate the involvement of PIP2 in the processes during the C. elegans development, we identified the PIP2-binding partners, leucine-rich repeat (LRR-1) protein and proteasome subunit beta 4 (PBS-4), pointing to its involvement in the ubiquitin–proteasome pathway.
Schlagwörter	nucleus ; phosphatidylinositol 4,5-bisphosphate ; PPK-1 ; C. elegans ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Thema/Rubrik (Code)	571
Sprache	Englisch
Erscheinungsdatum	2018-09-01T00:00:00Z
Verlag	MDPI AG
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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Artikel ; Online: Nuclear myosin I regulates cell membrane tension.

Venit, Tomáš / Kalendová, Alžběta / Petr, Martin / Dzijak, Rastislav / Pastorek, Lukáš / Rohožková, Jana / Malohlava, Jakub / Hozák, Pavel

Scientific reports

2016 Band 6, Seite(n) 30864

Abstract: Plasma membrane tension is an important feature that determines the cell shape and influences processes such as cell motility, spreading, endocytosis and exocytosis. Unconventional class 1 myosins are potent regulators of plasma membrane tension because ... ...

Abstract	Plasma membrane tension is an important feature that determines the cell shape and influences processes such as cell motility, spreading, endocytosis and exocytosis. Unconventional class 1 myosins are potent regulators of plasma membrane tension because they physically link the plasma membrane with adjacent cytoskeleton. We identified nuclear myosin 1 (NM1) - a putative nuclear isoform of myosin 1c (Myo1c) - as a new player in the field. Although having specific nuclear functions, NM1 localizes predominantly to the plasma membrane. Deletion of NM1 causes more than a 50% increase in the elasticity of the plasma membrane around the actin cytoskeleton as measured by atomic force microscopy. This higher elasticity of NM1 knock-out cells leads to 25% higher resistance to short-term hypotonic environment and rapid cell swelling. In contrast, overexpression of NM1 in wild type cells leads to an additional 30% reduction of their survival. We have shown that NM1 has a direct functional role in the cytoplasm as a dynamic linker between the cell membrane and the underlying cytoskeleton, regulating the degree of effective plasma membrane tension.
Mesh-Begriff(e)	Actin Cytoskeleton/metabolism ; Animals ; Cell Membrane/metabolism ; Cell Movement ; Cell Nucleus/metabolism ; Cell Shape ; Cells, Cultured ; Exocytosis/physiology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; HeLa Cells ; Humans ; Mice ; Mice, Knockout ; Myosin Type I/metabolism ; Skin/cytology ; Skin/metabolism
Chemische Substanzen	Myosin Type I (EC 3.6.1.-)
Sprache	Englisch
Erscheinungsdatum	2016--02
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep30864
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus.

Venit, Tomáš / Dzijak, Rastislav / Kalendová, Alžběta / Kahle, Michal / Rohožková, Jana / Schmidt, Volker / Rülicke, Thomas / Rathkolb, Birgit / Hans, Wolfgang / Bohla, Alexander / Eickelberg, Oliver / Stoeger, Tobias / Wolf, Eckhard / Yildirim, Ali Önder / Gailus-Durner, Valérie / Fuchs, Helmut / de Angelis, Martin Hrabě / Hozák, Pavel

PloS one

2013 Band 8, Heft 4, Seite(n) e61406

Abstract: Background: Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 ... ...

Abstract	Background: Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 amino acids at the N-terminus. Previous studies revealed its roles in RNA Polymerase I and RNA Polymerase II transcription, chromatin remodeling, and chromosomal movements. Its nuclear localization signal is localized in the middle of the molecule and therefore directs both Myosin 1c isoforms to the nucleus. Methodology/principal findings: In order to trace specific functions of the NM1 isoform, we generated mice lacking the NM1 start codon without affecting the cytoplasmic Myo1c protein. Mutant mice were analyzed in a comprehensive phenotypic screen in cooperation with the German Mouse Clinic. Strikingly, no obvious phenotype related to previously described functions has been observed. However, we found minor changes in bone mineral density and the number and size of red blood cells in knock-out mice, which are most probably not related to previously described functions of NM1 in the nucleus. In Myo1c/NM1 depleted U2OS cells, the level of Pol I transcription was restored by overexpression of shRNA-resistant mouse Myo1c. Moreover, we found Myo1c interacting with Pol II. The ratio between Myo1c and NM1 proteins were similar in the nucleus and deletion of NM1 did not cause any compensatory overexpression of Myo1c protein. Conclusion/significance: We observed that Myo1c can replace NM1 in its nuclear functions. Amount of both proteins is nearly equal and NM1 knock-out does not cause any compensatory overexpression of Myo1c. We therefore suggest that both isoforms can substitute each other in nuclear processes.
Mesh-Begriff(e)	Animals ; Blotting, Western ; Cell Nucleus/metabolism ; DNA Primers/genetics ; Genotype ; Immunoprecipitation ; Mice ; Mice, Knockout ; Myosin Type I/genetics ; Myosin Type I/metabolism ; Phenotype ; Plasmids/genetics ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Reverse Transcriptase Polymerase Chain Reaction
Chemische Substanzen	DNA Primers ; Myo1c protein, mouse ; Protein Isoforms ; Myosin Type I (EC 3.6.1.-)
Sprache	Englisch
Erscheinungsdatum	2013-04-11
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0061406
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus.

Tomáš Venit / Rastislav Dzijak / Alžběta Kalendová / Michal Kahle / Jana Rohožková / Volker Schmidt / Thomas Rülicke / Birgit Rathkolb / Wolfgang Hans / Alexander Bohla / Oliver Eickelberg / Tobias Stoeger / Eckhard Wolf / Ali Önder Yildirim / Valérie Gailus-Durner / Helmut Fuchs / Martin Hrabě de Angelis / Pavel Hozák

PLoS ONE, Vol 8, Iss 4, p e

2013 Band 61406

Abstract: BACKGROUND: Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 amino ...

Abstract	BACKGROUND: Nuclear myosin I (NM1) is a nuclear isoform of the well-known "cytoplasmic" Myosin 1c protein (Myo1c). Located on the 11(th) chromosome in mice, NM1 results from an alternative start of transcription of the Myo1c gene adding an extra 16 amino acids at the N-terminus. Previous studies revealed its roles in RNA Polymerase I and RNA Polymerase II transcription, chromatin remodeling, and chromosomal movements. Its nuclear localization signal is localized in the middle of the molecule and therefore directs both Myosin 1c isoforms to the nucleus. METHODOLOGY/PRINCIPAL FINDINGS: In order to trace specific functions of the NM1 isoform, we generated mice lacking the NM1 start codon without affecting the cytoplasmic Myo1c protein. Mutant mice were analyzed in a comprehensive phenotypic screen in cooperation with the German Mouse Clinic. Strikingly, no obvious phenotype related to previously described functions has been observed. However, we found minor changes in bone mineral density and the number and size of red blood cells in knock-out mice, which are most probably not related to previously described functions of NM1 in the nucleus. In Myo1c/NM1 depleted U2OS cells, the level of Pol I transcription was restored by overexpression of shRNA-resistant mouse Myo1c. Moreover, we found Myo1c interacting with Pol II. The ratio between Myo1c and NM1 proteins were similar in the nucleus and deletion of NM1 did not cause any compensatory overexpression of Myo1c protein. CONCLUSION/SIGNIFICANCE: We observed that Myo1c can replace NM1 in its nuclear functions. Amount of both proteins is nearly equal and NM1 knock-out does not cause any compensatory overexpression of Myo1c. We therefore suggest that both isoforms can substitute each other in nuclear processes.
Schlagwörter	Medicine ; R ; Science ; Q
Thema/Rubrik (Code)	570
Sprache	Englisch
Erscheinungsdatum	2013-01-01T00:00:00Z
Verlag	Public Library of Science (PLoS)
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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