ArticleMolecular and cellular biology1992
Distal protein sequences can affect the function of a nuclear localization signal.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.PLoS pathogens · 2018Article
- ICP8 Filament Formation Is Essential for Replication Compartment Formation during Herpes Simplex Virus Infection.Journal of virology · 2015Article
- Article
- Mutations in the beta-tubulin gene TUBB2B result in asymmetrical polymicrogyria.Nature genetics · 2009Article
- The bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.Journal of molecular biology · 2009Article
- Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.Journal of virology · 2003Article
- Specific inhibition of bovine viral diarrhea virus replicase.Journal of virology · 2003Article
- The 60-residue C-terminal region of the single-stranded DNA binding protein of herpes simplex virus type 1 is required for cooperative DNA binding.Journal of virology · 2000Article
- A beta-stranded motif drives capsid protein oligomers of the parvovirus minute virus of mice into the nucleus for viral assembly.Journal of virology · 2000Article
- Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.Molecular biology of the cell · 1999Article
- Formation of herpes simplex virus type 1 replication compartments by transfection: requirements and localization to nuclear domain 10.Journal of virology · 1997Article
- Functions of the tobacco etch virus RNA polymerase (NIb): subcellular transport and protein-protein interaction with VPg/proteinase (NIa).Journal of virology · 1997Article
- Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures.Journal of virology · 1996Article
- Characterization of nuclear structures in cells infected with herpes simplex virus type 1 in the absence of viral DNA replication.Journal of virology · 1996Article
- Nuclear and nucleolar targeting of human ribosomal protein S6.Molecular biology of the cell · 1995Article
- The N-terminus of fission yeast DNA polymerase alpha contains a basic pentapeptide that acts in vivo as a nuclear localization signal.Molecular biology of the cell · 1995Article
- Arginine-rich regions succeeding the nuclear localization region of the herpes simplex virus type 1 regulatory protein ICP27 are required for efficient nuclear localization and late gene expression.Journal of virology · 1995Article
- Nuclear localization signals overlap DNA- or RNA-binding domains in nucleic acid-binding proteins.Nucleic acids research · 1995Review
- Splinkerettes--improved vectorettes for greater efficiency in PCR walking.Nucleic acids research · 1995Article
- Identification of nuclear and nucleolar localization signals in the herpes simplex virus regulatory protein ICP27.Journal of virology · 1995Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The major DNA-binding protein, or infected-cell protein 8 (ICP8), encoded by herpes simplex virus can localize to the cell nucleus independently of other viral proteins. To define the nuclear localization signals within ICP8, we performed several forms of mutagenesis on the cloned ICP8 gene. Deletion analysis of the ICP8 gene showed that several portions of ICP8 are involved in its nuclear localization. To determine whether these regions were independent localization signals, we introduced various portions of the ICP8 gene into a series of cassette plasmids which allowed expression of fusion proteins containing pyruvate kinase, normally a cytoplasmic protein, fused to various portions of ICP8. These results showed that the carboxyl-terminal 28 residues are the only portion of ICP8 capable of targeting protein kinase into the nucleus. However, inclusion of certain additional regions of ICP8 into the fusion protein led to an inhibition of nuclear localization. Therefore, the carboxyl-terminal 28 residues of ICP8 can act independently as a nuclear localization signal, but certain conformational constraints or folding or assembly requirements in the remainder of the protein can affect the nuclear localization of the protein. Our results demonstrate that sequences distant from a nuclear localization signal can affect its ability to function. A set of fusion vectors has been isolated which should be of general use for making 5' or 3' fusions in any reading frame to rapidly map localization signals.
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