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The nucleic acid data:
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IRESite record type:
natural_transcript
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IRESs:
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IRES:
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IRES trans-acting factor (ITAFS):
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IRES trans-acting factor (ITAF):
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Type of the interaction between ITAF and the RNA subject to translation: direct_interaction_with_rna
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ITAF protein characteristics:
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ITAF abbreviated name: PTB
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ITAF fullname: polypyrimidine-tract binding protein (unspecified isoform)
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ITAF description (long): polypyrimidine-tract binding protein
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3.1.2. Organisms or in vitro systems where this ITAF was functionally studied:
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Organism or in vitro system where ITAF was shown:
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Necessity of ITAF for translation in this particular organism or system: required_and_must_be_supplemented
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Method used to demonstrate ITAF effect: in_vitro
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In vitro system used to demonstrate ITAF effect: rabbit reticulocytes lysate
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Organism or in vitro system where ITAF was shown:
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Necessity of ITAF for translation in this particular organism or system: required_but_available_internally
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Method used to demonstrate ITAF effect: in_vivo
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The organism where action of this ITAF was studied:
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Homo sapiens |
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Remarks:
Transfected BS-C-1 cells transcripts co-expressing PTB produced 12-fold more reporter protein but only 2.4x
more in HeLa cells which contain more of endogenous PTB (Gosert et al., 2000).
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Citations:
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Hunt S. L., Hsuan J. J., Totty N., Jackson R. J. (1999) unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes. Dev. 13(4):437-448 |
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Gosert R, Chang KH, Rijnbrand R, Yi M, Sangar DV, Lemon SM (2000) Transient expression of cellular polypyrimidine-tract binding protein stimulates cap-independent translation directed by both picornaviral and flaviviral internal ribosome entry sites In vivo. Mol. Cell. Biol. 20(5):1583-1595 |
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IRES trans-acting factor (ITAF):
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Type of the interaction between ITAF and the RNA subject to translation: direct_interaction_with_rna
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ITAF protein characteristics:
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ITAF abbreviated name: Unr
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ITAF fullname: upstream of N-ras
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ITAF description (long): Unr protein is known to bind to gaagaaguaa
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3.2.2. Organisms or in vitro systems where this ITAF was functionally studied:
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Organism or in vitro system where ITAF was shown:
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Necessity of ITAF for translation in this particular organism or system: required_but_available_internally
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Method used to demonstrate ITAF effect: in_vivo
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Citations:
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IRES trans-acting factor (ITAF):
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Type of the interaction between ITAF and the RNA subject to translation: direct_interaction_with_rna
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OPTIONAL: The interacting RNA base range (if any): 1-95,230-430
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ITAF protein characteristics:
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ITAF abbreviated name: PCBP-2
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ITAF fullname: poly(rC)-binding protein 2 (39 kDa)
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ITAF description (long): Required for poliovirus IRES activity (Blyn et al. 1996 and 1997) and replication (Toyoda et al., 2007). Its
amount is not limiting in rabbit reticulocyte lysates (RRL) (Hunt and Jackson 1999).
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3.3.2. Organisms or in vitro systems where this ITAF was functionally studied:
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Organism or in vitro system where ITAF was shown:
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Necessity of ITAF for translation in this particular organism or system: required_but_available_internally
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Method used to demonstrate ITAF effect: in_vitro
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In vitro system used to demonstrate ITAF effect: rabbit reticulocytes lysate
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Remarks:
Cytosines in regions 93-95 and 98-100 are required for viral replication while not translation although they
are present in the cloverleaf structure in region 1-89 (Toyoda et al., 2007).
PCBP2 also binds to domain IV of PV IRES and is required for ts activity (Blyn et al., 1996, 1997; Gamarnik et
al., 1997; Walter et al., 2002). Blyn et al. (1997) reported that PCBP1 cannot functionally replace PCBP2 in
HeLa cells in respect to translation initiation. This is in agreement with Walter et al. (2002) who reported
that PCBP1 can replace PCBP2 only in respect to replication.
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Citations:
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Hunt S. L., Jackson R. J. (1999) Polypyrimidine-tract binding protein (PTB) is necessary, but not sufficient, for efficient internal initiation of translation of human rhinovirus-2 RNA. RNA. 5(3):344-359 |
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Toyoda H, Franco D, Fujita K, Paul AV, Wimmer E (2007) Replication of poliovirus requires binding of the poly(rC) binding protein to the cloverleaf as well as to the adjacent C-rich spacer sequence between the cloverleaf and the internal ribosomal entry site. J. Virol. 81(18):10017-10028 |
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Blyn LB, Swiderek KM, Richards O, Stahl DC, Semler BL, Ehrenfeld E (1996) Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 93(20):11115-11120 |
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Blyn LB, Towner JS, Semler BL, Ehrenfeld E (1997) Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA. J. Virol. 71(8):6243-6246 |
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Gamarnik AV, Andino R (1997) Two functional complexes formed by KH domain containing proteins with the 5' noncoding region of poliovirus RNA. RNA. 3(8):882-892 |
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Walter BL, Parsley TB, Ehrenfeld E, Semler BL (2002) Distinct poly(rC) binding protein KH domain determinants for poliovirus translation initiation and viral RNA replication. J. Virol. 76(23):12008-12022 |
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IRES trans-acting factor (ITAF):
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Type of the interaction between ITAF and the RNA subject to translation: direct_interaction_with_rna
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ITAF protein characteristics:
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ITAF abbreviated name: La
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ITAF fullname: La autoantigen
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ITAF description (long): La autoantigen (p52), 52 kDa RNA binding protein, predominantly localized to nucleus, unwinds the dsRNA in
ATP-dependent manner, forms a dimer
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3.4.2. Organisms or in vitro systems where this ITAF was functionally studied:
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Organism or in vitro system where ITAF was shown:
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Necessity of ITAF for translation in this particular organism or system: required_but_available_internally_although_in_limiting_concentration
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Method used to demonstrate ITAF effect: in_vitro
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In vitro system used to demonstrate ITAF effect: rabbit reticulocytes lysate
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Citations:
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Craig AW, Svitkin YV, Lee HS, Belsham GJ, Sonenberg N (1997) The La autoantigen contains a dimerization domain that is essential for enhancing translation. Mol. Cell. Biol. 1(17):163-169 |
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Meerovitch K, Svitkin YV, Lee HS, Lejbkowicz F, Kenan DJ, Chan EK, Agol VI, Keene JD, Sonenberg N (1993) La autoantigen enhances and corrects aberrant translation of poliovirus RNA in reticulocyte lysate. J. Virol. 7(67):3798-3807 |
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Svitkin YV, Meerovitch K, Lee HS, Dholakia JN, Kenan DJ, Agol VI, Sonenberg N (1994) Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro. J. Virol. 3(68):1544-1550 |
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Regions with experimentally determined secondary structures:
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A region with the experimentally determined secondary structure:
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