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Titolo:
Recognition of 5 '-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2
Autore:
Ben-Asouli, Y; Banai, Y; Hauser, H; Kaempfer, R;
Indirizzi:
Hebrew Univ Jerusalem, Hadassah Med Sch, Dept Mol Virol, IL-91120 Jerusalem, Israel Hebrew Univ Jerusalem Jerusalem Israel IL-91120 -91120 Jerusalem, Israel GBF, Natl Res Inst Biotechnol, Dept Gene Regulat & Differentiat, D-38124 Braunschweig, Germany GBF Braunschweig Germany D-38124 erentiat, D-38124 Braunschweig, Germany
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 4, volume: 28, anno: 2000,
pagine: 1011 - 1018
SICI:
0305-1048(20000215)28:4<1011:RO5'TS>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSACTIVATION RESPONSE ELEMENT; ACTIVATED PROTEIN-KINASE; MESSENGER-RNA; FACTOR-II; TRANS-ACTIVATION; BINDING-PROTEIN; MAMMALIAN-CELLS; BETA-SUBUNIT; GENOMIC RNA; REGION RNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Kaempfer, R Hebrew Univ Jerusalem, Hadassah Med Sch, Dept Mol Virol, IL-91120 Jerusalem, Israel Hebrew Univ Jerusalem Jerusalem Israel IL-91120 alem, Israel
Citazione:
Y. Ben-Asouli et al., "Recognition of 5 '-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2", NUCL ACID R, 28(4), 2000, pp. 1011-1018

Abstract

TAR, a 59 nt 5'-terminal hairpin in human immunodeficiency virus 1 (HIV-1)mRNA, binds viral Tat and several cellular proteins, We report that eukaryotic translation initiation factor 2 (elF2) recognizes TAR. TAR and the AUGinitiation codon domain, located well downstream from TAR, both contributeto the affinity of HIV-1 mRNA for elF2, The affinity of TAR for elF2 was insensitive to lower stem mutations that modify sequence and structure or tosequence changes throughout the remainder that leave the TAR secondary structure intact, Hence, elF2 recognizes structure rather than sequence in TAR. The affinity for elF2 was severely reduced by a 3 nt change that convertsthe single A bulge into a 7 nt internal loop. T1 footprinting showed that elF2 protects nucleotides in the loop as well as in the strand opposite theA bulge, Thus, elF2 recognizes the TAR loop and lower part of the sub-apical stem, Though not contiguous, these regions are brought into proximity inTAR by a bend in the helical structure induced by the UCU bulge; binding of elF2 opens up the bulge context and apical stem. The ability to bind elF2suggests a function for TAR in HIV-1 mRNA translation, Indeed, the 3 nt change that reduces the affinity of TAR for elF2 impairs the ability of reporter mRNA to compete in translation, Interaction of TAR with elF2 thus allows HIV-1 mRNA to compete more effectively during protein synthesis.

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Documento generato il 21/09/20 alle ore 02:22:41