PMID- 10049359
OWN - NLM
STAT- MEDLINE
DCOM- 19990420
LR  - 20200304
IS  - 0890-9369 (Print)
IS  - 0890-9369 (Linking)
VI  - 13
IP  - 4
DP  - 1999 Feb 15
TI  - unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is 
      required for internal initiation of translation of human rhinovirus RNA.
PG  - 437-48
AB  - Initiation of translation of the animal picornavirus RNAs occurs via a mechanism 
      of direct ribosome entry, which requires a segment of the 5' UTR of the RNA,
      known as the internal ribosome entry site (IRES). In addition, translation of the
      enterovirus and rhinovirus (HRV) subgroups requires cellular trans-acting factors
      that are absent from, or limiting in rabbit reticulocytes, but are more abundant 
      in HeLa cell extracts. It has been shown previously that HeLa cells contain two
      separable activities, each of which independently stimulates HRV IRES-dependent
      translation when used to supplement reticulocyte lysate; one of these activities 
      was identified as polypyrimidine tract-binding protein (PTB). Here, the
      purification of the second activity is achieved by use of an RNA-affinity column 
      based on the HRV 5' UTR. It comprises two components: a 38-kD protein (p38),
      which is a novel member of the GH-WD repeat protein family and has no intrinsic
      RNA-binding activity; and a 96- to 97-kD protein doublet, which was identified as
      unr, an RNA-binding protein with five cold-shock domains. Coimmunoprecipitation
      with antibodies against either protein shows that the two proteins interact with 
      each other, and thus p38 is named unrip (unr-interacting protein). Recombinant
      unr acts synergistically with recombinant PTB to stimulate translation dependent 
      on the rhinovirus IRES. In contrast, unr did not significantly augment the
      PTB-dependent stimulation of poliovirus IRES activity.
FAU - Hunt, S L
AU  - Hunt SL
AD  - Department of Biochemistry, University of Cambridge, Old Addenbrooke's Site,
      Cambridge, CB2 1GA, UK.
FAU - Hsuan, J J
AU  - Hsuan JJ
FAU - Totty, N
AU  - Totty N
FAU - Jackson, R J
AU  - Jackson RJ
LA  - eng
SI  - GENBANK/AJ010025
GR  - WT_/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Genes Dev
JT  - Genes & development
JID - 8711660
RN  - 0 (5' Untranslated Regions)
RN  - 0 (CSDE1 protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Extracts)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Viral)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (STRAP protein, human)
RN  - 139076-35-0 (Polypyrimidine Tract-Binding Protein)
SB  - IM
MH  - 5' Untranslated Regions/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carrier Proteins/*genetics
MH  - Cell Extracts/chemistry
MH  - DNA-Binding Proteins/*genetics/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - *Neoplasm Proteins
MH  - Poliovirus/genetics
MH  - Polypyrimidine Tract-Binding Protein
MH  - Precipitin Tests
MH  - Protein Binding/genetics
MH  - Protein Biosynthesis/*genetics
MH  - RNA, Messenger/metabolism
MH  - RNA, Viral/*genetics
MH  - RNA-Binding Proteins/*genetics/metabolism
MH  - Rabbits
MH  - Recombinant Proteins/metabolism
MH  - Reticulocytes/metabolism
MH  - Rhinovirus/*genetics
MH  - Sequence Analysis, DNA
PMC - PMC316477
EDAT- 1999/02/27 00:00
MHDA- 1999/02/27 00:01
CRDT- 1999/02/27 00:00
PHST- 1999/02/27 00:00 [pubmed]
PHST- 1999/02/27 00:01 [medline]
PHST- 1999/02/27 00:00 [entrez]
AID - 10.1101/gad.13.4.437 [doi]
PST - ppublish
SO  - Genes Dev. 1999 Feb 15;13(4):437-48. doi: 10.1101/gad.13.4.437.