The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus. / Evans, Sharon A.; Belsham, Graham J.; Barrett, Thomas.

I: Virology, Bind 177, Nr. 1, 07.1990, s. 317-323.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Evans, SA, Belsham, GJ & Barrett, T 1990, 'The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus', Virology, bind 177, nr. 1, s. 317-323. https://doi.org/10.1016/0042-6822(90)90486-B

APA

Evans, S. A., Belsham, G. J., & Barrett, T. (1990). The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus. Virology, 177(1), 317-323. https://doi.org/10.1016/0042-6822(90)90486-B

Vancouver

Evans SA, Belsham GJ, Barrett T. The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus. Virology. 1990 jul.;177(1):317-323. https://doi.org/10.1016/0042-6822(90)90486-B

Author

Evans, Sharon A. ; Belsham, Graham J. ; Barrett, Thomas. / The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus. I: Virology. 1990 ; Bind 177, Nr. 1. s. 317-323.

Bibtex

@article{c5a7c6e0b57b457a8ed767a95996895a,
title = "The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus",
abstract = "The mRNAs which code for the fusion proteins of the morbilliviruses (measles virus, canine distemper virus, and rinderpest virus) have unusually long 5′ untranslated regions (UTRs) which are GC-rich and are capable of folding into extensive secondary structures. In measles virus the first AUG codons in the fusion (F) protein mRNA are in close proximity at nucleotide positions 574 and 583 and protein translation is initiated at the second position. In the canine distemper virus (CDV) and rinderpest virus (RPV) F gene transcripts the analogous initiation codons are preceded by several other AUG codons many nucleotides upstream either in the same reading frame or at the beginning of other short open reading frames. We have studied the effect of deleting these upstream regions on the production of the fusion proteins of both CDV and RPV from cDNA constructs. Within the cells the presence of these regions enhances the production of the F protein while, in contrast, the production of the authentic F protein from in vitro translations using RNA transcripts is inhibited by these sequences.",
author = "Evans, {Sharon A.} and Belsham, {Graham J.} and Thomas Barrett",
note = "Funding Information: We thank Dr. B. Moss (NIH) for the gift of vTF7-3 and Dr. B. Rima (QUB, Northern Ireland) for the CDV antiserum. The work was supported in part by Wellcome Trust Grant 14294/l .5 (T.B. and S.A.E.). We also thank L. Goatley and J. K. Brangwyn fortechnical assistance.",
year = "1990",
month = jul,
doi = "10.1016/0042-6822(90)90486-B",
language = "English",
volume = "177",
pages = "317--323",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press",
number = "1",

}

RIS

TY - JOUR

T1 - The role of the 5′ nontranslated regions of the fusion protein mRNAs of canine distemper virus and rinderpest virus

AU - Evans, Sharon A.

AU - Belsham, Graham J.

AU - Barrett, Thomas

N1 - Funding Information: We thank Dr. B. Moss (NIH) for the gift of vTF7-3 and Dr. B. Rima (QUB, Northern Ireland) for the CDV antiserum. The work was supported in part by Wellcome Trust Grant 14294/l .5 (T.B. and S.A.E.). We also thank L. Goatley and J. K. Brangwyn fortechnical assistance.

PY - 1990/7

Y1 - 1990/7

N2 - The mRNAs which code for the fusion proteins of the morbilliviruses (measles virus, canine distemper virus, and rinderpest virus) have unusually long 5′ untranslated regions (UTRs) which are GC-rich and are capable of folding into extensive secondary structures. In measles virus the first AUG codons in the fusion (F) protein mRNA are in close proximity at nucleotide positions 574 and 583 and protein translation is initiated at the second position. In the canine distemper virus (CDV) and rinderpest virus (RPV) F gene transcripts the analogous initiation codons are preceded by several other AUG codons many nucleotides upstream either in the same reading frame or at the beginning of other short open reading frames. We have studied the effect of deleting these upstream regions on the production of the fusion proteins of both CDV and RPV from cDNA constructs. Within the cells the presence of these regions enhances the production of the F protein while, in contrast, the production of the authentic F protein from in vitro translations using RNA transcripts is inhibited by these sequences.

AB - The mRNAs which code for the fusion proteins of the morbilliviruses (measles virus, canine distemper virus, and rinderpest virus) have unusually long 5′ untranslated regions (UTRs) which are GC-rich and are capable of folding into extensive secondary structures. In measles virus the first AUG codons in the fusion (F) protein mRNA are in close proximity at nucleotide positions 574 and 583 and protein translation is initiated at the second position. In the canine distemper virus (CDV) and rinderpest virus (RPV) F gene transcripts the analogous initiation codons are preceded by several other AUG codons many nucleotides upstream either in the same reading frame or at the beginning of other short open reading frames. We have studied the effect of deleting these upstream regions on the production of the fusion proteins of both CDV and RPV from cDNA constructs. Within the cells the presence of these regions enhances the production of the F protein while, in contrast, the production of the authentic F protein from in vitro translations using RNA transcripts is inhibited by these sequences.

UR - http://www.scopus.com/inward/record.url?scp=0025289847&partnerID=8YFLogxK

U2 - 10.1016/0042-6822(90)90486-B

DO - 10.1016/0042-6822(90)90486-B

M3 - Journal article

C2 - 2353458

AN - SCOPUS:0025289847

VL - 177

SP - 317

EP - 323

JO - Virology

JF - Virology

SN - 0042-6822

IS - 1

ER -

ID: 381223646