The genome of all retrovirus consists of two copies of genomic RNA which are noncovalently linked near their 5' end. A sequence localized immediately upstream from the splice donor site inside the HIV-1 psi-RNA region was identified as the domain responsible for the dimerization initiation. It was shown that a kissing complex and a stable dimer are both involved in the HIV-1Lai RNA dimerization process in vitro. The NCp7 protein activates the dimerization by converting a transient loop-loop complex into a more stable dimer. The structure of this transitory loop-loop complex was recently elucidated by Mujeeb et al. In work presented here, we use NMR spectroscopy to determine the stable extended dimer structure formed from a 23 nucleotides RNA fragment, part of the 35 nucleotides SL1 sequence. By heating to 90 degrees C, then slowly cooling this sequence, we were able to show that an extended dimer is formed. We present evidence for the three dimensional structure of this dimer. NMR data yields evidence for a zipper like motif A8A9.A16 existence. This motif enables the surrounding bases to be positioned more closely and permit the G7 and C17 bases to be paired. This is different to other related sequences where only the kissing complex is observed, we suggest that the zipper like motif AA.A could be an important stabilization factor of the extended duplex.
NMR Specialist Genomic Biology
NMR Specialist Genomic Biology
The Institute for Genomic Biology has a position open for a NMR Specialist.
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[NMR paper] NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Related Articles NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Biochemistry. 2004 Nov 30;43(47):14940-7
Authors: Biverståhl H, Andersson A, Gräslund A, Mäler L
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy...
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11-24-2010 10:03 PM
[NMR paper] Structure and dynamics of translation initiation factor aIF-1A from the archaeon Meth
Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy.
Related Articles Structure and dynamics of translation initiation factor aIF-1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy.
Protein Sci. 2001 Dec;10(12):2426-38
Authors: Li W, Hoffman DW
Translation initiation factor 1A (aIF-1A) from the archaeon Methanococcus jannaschii was expressed in Escherichia coli, purified, and characterized in terms of its structure and dynamics using...
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11-19-2010 08:44 PM
[NMR paper] Solution structure of the conserved segment of the Myb cognate DNA sequence by 2D NMR
Solution structure of the conserved segment of the Myb cognate DNA sequence by 2D NMR, spectral simulation, restrained energy minimization, and distance geometry calculations.
Related Articles Solution structure of the conserved segment of the Myb cognate DNA sequence by 2D NMR, spectral simulation, restrained energy minimization, and distance geometry calculations.
Biochemistry. 1995 May 2;34(17):5913-22
Authors: Radha PK, Madan A, Nibedita R, Hosur RV
Solution structure of a self-complementary DNA duplex d-ACCGTTAACGGT containing the TAACGG...
[NMR paper] Sequence-specific 1H NMR assignments and secondary structure in solution of Escherich
Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Related Articles Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Biochemistry. 1990 Jul 10;29(27):6332-41
Authors: Arrowsmith CH, Pachter R, Altman RB, Iyer SB, Jardetzky O
Sequence-specific 1H NMR assignments are reported for the active L-tryptophan-bound form of Escherichia coli trp repressor. The repressor is a symmetric dimer of 107 residues per monomer; thus at 25 kDa, this...
Dimer initiation sequence of HIV-1Lai genomic RNA: NMR solution structure of the exte
Linear Mode
