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Michael Wegner - One of the best experts on this subject based on the ideXlab platform.
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Structural requirements for Nuclear Localization of GCMa/Gcm‐1
FEBS letters, 2003Co-Authors: Said Hashemolhosseini, Karin Kilian, Elena Kardash, Peter Lischka, Thomas Stamminger, Michael WegnerAbstract:GCM proteins constitute a small transcription factor family. Nuclear Localization of Drosophila GCM is mediated by a typical bipartite Nuclear Localization sequence (NLS) close to the DNA-binding GCM domain. Here, we have analyzed Nuclear Localization of the mammalian GCM proteins. Whereas GCMb/Gcm-2 contained a classical bipartite NLS, Nuclear Localization of GCMa/Gcm-1 was mediated by two regions without resemblance to known NLS, one corresponding to the amino-terminal part of the GCM domain, the second defined as a tyrosine-and-proline-rich carboxy-terminal region. Nuclear import was counteracted by an amino-terminal Nuclear export activity. This complex regulation of subcellular Localization has important implications for GCMa/Gcm-1 function.
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identification of the Nuclear Localization signal of the pou domain protein tst 1 oct6
Journal of Biological Chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:Abstract POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
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Identification of the Nuclear Localization Signal of the POU Domain Protein Tst-1/Oct6 *
The Journal of biological chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
Elisabeth Sock - One of the best experts on this subject based on the ideXlab platform.
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identification of the Nuclear Localization signal of the pou domain protein tst 1 oct6
Journal of Biological Chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:Abstract POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
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Identification of the Nuclear Localization Signal of the POU Domain Protein Tst-1/Oct6 *
The Journal of biological chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
Janna Enderich - One of the best experts on this subject based on the ideXlab platform.
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identification of the Nuclear Localization signal of the pou domain protein tst 1 oct6
Journal of Biological Chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:Abstract POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
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Identification of the Nuclear Localization Signal of the POU Domain Protein Tst-1/Oct6 *
The Journal of biological chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
Michael G. Rosenfeld - One of the best experts on this subject based on the ideXlab platform.
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identification of the Nuclear Localization signal of the pou domain protein tst 1 oct6
Journal of Biological Chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:Abstract POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
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Identification of the Nuclear Localization Signal of the POU Domain Protein Tst-1/Oct6 *
The Journal of biological chemistry, 1996Co-Authors: Elisabeth Sock, Janna Enderich, Michael G. Rosenfeld, Michael WegnerAbstract:POU domain proteins are important regulators of development and terminal differentiation based upon their transcriptional activity in the nucleus. Here, we analyzed the mechanism underlying the Nuclear Localization of Tst-1/Oct6, a member of this family that regulates events during neurogenesis and myelination. Nuclear Localization of Tst-1/Oct6 was dependent on the POU domain, as its deletion prevented access to the nucleus, whereas its transfer to the amino terminus of β-galactosidase was sufficient to prompt Nuclear accumulation of this normally cytosolic protein. Interestingly, Nuclear Localization and high affinity DNA binding were two independent functions of the POU domain and could be separated in several mutants. While specific high affinity binding to DNA required the presence of both the POU-specific and the POU homeodomain, the POU-specific domain was dispensable for Nuclear Localization of Tst-1/Oct6. Rather, the Nuclear Localization function was selectively contained within the POU homeodomain. Specifically, a basic cluster (GRKRKKRT) preceding helix 1 of the homeodomain was shown by deletion mutagenesis to be involved in the Nuclear Localization of Tst-1/Oct6. This sequence, which is highly conserved among POU domain proteins, was by itself capable of translocating β-galactosidase to the nucleus defining it as the bona fide Nuclear Localization signal of Tst-1/Oct6 and presumably other POU domain factors.
Aurelio Garcia - One of the best experts on this subject based on the ideXlab platform.
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Enhancement of polyhedrin Nuclear Localization during baculovirus infection.
Journal of virology, 1992Co-Authors: Donald L Jarvis, Dwight Bohlmeyer, Aurelio GarciaAbstract:Polyhedrin is the major component of the Nuclear viral occlusions produced during replication of the baculovirus Autographa californica multicapsid Nuclear polyhedrosis virus (AcMNPV). Since viral occlusions are responsible for the horizontal transmission of AcMNPV in nature, the biosynthesis, Localization, and assembly of polyhedrin are important events in the viral replication cycle. We recently defined the sequence requirements for Nuclear Localization and assembly of polyhedrin. In this study, we examined the Localization of polyhedrin at different times of infection. The results showed that Nuclear Localization of polyhedrin becomes more efficient as the occlusion phase of infection progresses. Several different factors were identified that might contribute to this overall effect, including a higher rate of polyhedrin Nuclear Localization and a higher rate of polyhedrin biosynthesis. We also examined the biosynthesis and processing of polyhedrin in cells infected with an AcMNPV few polyhedra (FP) mutant, which produces smaller numbers of viral occlusions that contain few or no virions. Compared with wild type, the FP mutant produced polyhedrin more slowly and localized it to the nucleus less efficiently at the beginning of the occlusion phase of infection (24 h postinfection). This supported the idea that the efficiency of polyhedrin Nuclear Localization is tightly coupled to its rate of biosynthesis. It also revealed that expression of the viral 25K gene, which is inactivated in the FP mutant, is directly or indirectly associated with an enhancement of polyhedrin biosynthesis and Nuclear Localization at the beginning of the occlusion phase of infection. This enhancement effect appears to be necessary to ensure the normal assembly of viral occlusions.
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Enhancement of polyhedrin Nuclear Localization during baculovirus infection.
Journal of Virology, 1992Co-Authors: Donald L Jarvis, Dwight Bohlmeyer, Aurelio GarciaAbstract:Polyhedrin is the major component of the Nuclear viral occlusions produced during replication of the baculovirus Autographa californica multicapsid Nuclear polyhedrosis virus (AcMNPV). Since viral occlusions are responsible for the horizontal transmission of AcMNPV in nature, the biosynthesis, Localization, and assembly of polyhedrin are important events in the viral replication cycle. We recently defined the sequence requirements for Nuclear Localization and assembly of polyhedrin. In this study, we examined the Localization of polyhedrin at different times of infection. The results showed that Nuclear Localization of polyhedrin becomes more efficient as the occlusion phase of infection progresses. Several different factors were identified that might contribute to this overall effect, including a higher rate of polyhedrin Nuclear Localization and a higher rate of polyhedrin biosynthesis. We also examined the biosynthesis and processing of polyhedrin in cells infected with an AcMNPV few polyhedra (FP) mutant, which produces smaller numbers of viral occlusions that contain few or no virions. Compared with wild type, the FP mutant produced polyhedrin more slowly and localized it to the nucleus less efficiently at the beginning of the occlusion phase of infection (24 h postinfection). This supported the idea that the efficiency of polyhedrin Nuclear Localization is tightly coupled to its rate of biosynthesis. It also revealed that expression of the viral 25K gene, which is inactivated in the FP mutant, is directly or indirectly associated with an enhancement of polyhedrin biosynthesis and Nuclear Localization at the beginning of the occlusion phase of infection. This enhancement effect appears to be necessary to ensure the normal assembly of viral occlusions. Images
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Requirements for Nuclear Localization and supramolecular assembly of a baculovirus polyhedrin protein
Virology, 1991Co-Authors: Donald L Jarvis, Dwight Bohlmeyer, Aurelio GarciaAbstract:Abstract This study defines the requirements for the Nuclear Localization, stable Nuclear association, and supramolecular assembly of a baculovirus polyhedrin protein in lepidopteran insect cells. Fragments of the polyhedrin protein were genetically fused to two different nonNuclear reporter proteins and the intracellular distribution of the fusion proteins was analyzed in infected insect cells. Analysis by indirect immunofluorescence showed that the domain between amino acids 30 and 57 could mediate Nuclear Localization of polyhedrin. However, biochemical fractionation experiments showed that this domain was not sufficient for a detergent-stable association of polyhedrin with the nucleus. This required a slightly larger domain, between amino acids 30 and 110. Differential interference-contrast microscopy showed that the supramolecular assembly of polyhedrin into Nuclear occlusion-like particles required the domain between amino acids 19 and 110. The most likely candidate for a minimal Nuclear Localization signal was the sequence KRKK, located between amino acids 32 and 35. Therefore, oligonucleotide-directed mutagenesis was used to change this sequence to NGNN and the intracellular distribution of the mutant protein was analyzed. The results showed that the mutant protein was predominantly localized in the cytoplasm of infected cells, where it assembled into large, cubic, occlusion-like particles. Thus, the KRKK sequence is necessary for the Nuclear Localization of polyhedrin, but Nuclear Localization is not required for its supramolecular assembly into occlusion-like particles.
