In vitro membrane binding of the translation products of the carlavirus 7-kDa protein genes.
Two double-stranded DNA copies of the genes potentially coding for the 7-kDa proteins of potato virus M (PVM) and potato virus S (PVS) were synthesized and cloned into T7 transcription vectors. Cell-free translation of the corresponding monocistronic transcripts yielded in both cases a single protein of approximately 7-8 kDa that contains a highly hydrophobic N-terminal segment. To analyze their membrane-binding potential, both proteins were synthesized in the membrane-enriched Krebs-2 extract. It was found that the smooth membrane fraction was enriched in the carlavirus 7-kDa proteins. The primary and predicted secondary structures of their N-terminal hydrophobic segments suggest that the latter can function as signals for translocation into the rough endoplasmic reticulum.
Morozov
S Y
SY
Department of Virology, Moscow State University, USSR.
Miroshnichenko
N A
NA
Solovyev
A G
AG
Zelenina
D A
DA
Fedorkin
O N
ON
Lukasheva
L I
LI
Grachev
S A
SA
Chernov
B K
BK
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010942:Plant Viruses / Q000235:genetics* / Q000378:metabolism; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012328:RNA Viruses / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D011198:Solanum tuberosum; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism*
C069857:7 kDa protein, carlavirus; D008565:Membrane Proteins; D014764:Viral Proteins