Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition.

Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Research Abstract Details 

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Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Abstract Text:

Xiaoyan Sun,Qi Zhang,Hashim M Al-Hashimi,

Stem loop 1 (SL1) is a highly conserved hairpin in the 5'-leader of the human immunodeficiency virus type I that forms a metastable kissing dimer that is converted during viral maturation into a stable duplex with the aid of the nucleocapsid (NC) protein. SL1 contains a highly conserved internal loop that promotes the kissing-duplex transition by a mechanism that remains poorly understood. Using NMR, we characterized internal motions induced by the internal loop in an SL1 monomer that may promote the kissing-duplex transition. This includes micro-to-millisecond secondary structural transitions that cause partial melting of three base-pairs above the internal loop making them key nucleation sites for exchanging strands and nanosecond rigid-body stem motions that can help bring strands into spatial register. We show that while Mg2+ binds to the internal loop and arrests these internal motions, it preserves and/or activates local mobility at internal loop residues G272 and G273 which are implicated in NC binding. By stabilizing SL1 without compromising the accessibility of G272 and G273 for NC binding, Mg2+ may increase the dependence of the kissing-duplex transition on NC binding thus preventing spontaneous transitions from taking place and ensuring that viral RNA and protein maturation occur in concert.

Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Publishing Authors By Initials

X Sun,Q Zhang,HM Al-Hashimi,

For similar nucleic acids, nucleotides, and nucleosides: nucleic acids: rna: rna, viral research abstracts see: nucleic acids, nucleotides, and nucleosides: nucleic acids: rna: rna, viral research

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Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Nucleic acids research

VOLUME: 35

Page Numbers: 1698-713

Journal Abbreviation:

ISSN: 1362-4962

DAY: 20

MONTH: 02

YEAR: 2007

Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 411011

Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Keywords Mesh Terms:

KEYWORDS: RNA, Viral

MESH TERMS: chemistry

Chemical & Substance for Abstract: Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition. Information

Substance Name: Magnesium

Registry Number: 7439-95-4

Grant and Affiliation Information for Resolving fast and slow motions in the internal loop containing stem-loop 1 of HIV-1 that are modulated by Mg2+ binding: role in the kissing-duplex structural transition.

AFFILIATION: Department of Chemistry & Biophysics Research Division, The University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055, USA.

Country: England

AGENCY: United States NIAID

GRANT: R01 AI066975

ACRONYM: AI

MEDLINETA: Nucleic Acids Res

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