title: Herpes simplex virus type 2 UL14 gene product has heat shock protein (HSP)-like functions.
abstract: The HSV-2 UL14 gene encodes a 32 kDa protein that is a minor component of the viral tegument. The protein relocates other viral proteins such as VP26 and UL33 protein into the nuclei of transiently coexpressing cells (Yamauchi et al., 2001). We found that the protein shared some characteristics of heat shock proteins (HSPs) or molecular chaperones, such as nuclear translocation upon heat shock, ATP deprivation and osmotic shock. Interestingly, a significant homology over a stretch of 15 amino acids was found between an N-terminal region of HSV UL14 protein and the substrate-binding domain of Hsp70 family proteins. Two arginine residues in this region were important for nuclear translocation of VP26. In addition, overexpression of UL14 protein increased the activity of coexpressed firefly luciferase, which suggested that the protein functioned in the folding of newly synthesized luciferase. We thus conclude that UL14 protein can act as a chaperone-like protein in a singly expressed state.
authors.affiliation: Laboratory of Virology, Institute for Disease Mechanism and Control, Nagoya University School of Medicine, Tsurumai-cho 65, Showa-ku, Japan.
authors.forename: Yohei
authors.initials: Y
authors.lastname: Yamauchi
authors.forename: Kaoru
authors.initials: K
authors.lastname: Wada
authors.forename: Fumi
authors.initials: F
authors.lastname: Goshima
authors.forename: Tohru
authors.initials: T
authors.lastname: Daikoku
authors.forename: Kenzo
authors.initials: K
authors.lastname: Ohtsuka
authors.forename: Yukihiro
authors.initials: Y
authors.lastname: Nishiyama
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000595:Amino Acid Sequence / Q000502:physiology; D000818:Animals; D001120:Arginine / Q000378:metabolism; D002451:Cell Compartmentation / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism / Q000821:virology; D002522:Chlorocebus aethiops; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006561:Herpes Simplex / Q000378:metabolism* / Q000503:physiopathology; D018258:Herpesvirus 2, Human / Q000378:metabolism*; D006801:Humans; D008156:Luciferases / Q000235:genetics / Q000378:metabolism; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D016376:Oligonucleotides, Antisense; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport / Q000502:physiology; D014709:Vero Cells; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D016376:Oligonucleotides, Antisense; C402639:UL14 protein, Human herpesvirus 1; D014764:Viral Proteins; D001120:Arginine; D008156:Luciferases