Specific disulfide formation in the oxidation of HIV-1 zinc finger protein nucleocapsid p7. 1995

X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
Department of Chemistry and Biochemistry, University of Maryland Baltimore County 21228-5398, USA.

In vitro oxidation of the HIV-1 nucleocapsid protein p7 by the C-nitroso compound 3-nitrosobenzamide (NOBA) has been investigated. When reconstituted p7 was incubated with NOBA, three disulfide bonds were formed per molecule of p7, Cys 15-Cys 18, Cys 28-Cys 36, and Cys 39-Cys 49. These were identified using the proteolytic enzyme endoproteinase Lys-C and mass spectrometry. When the denatured protein (Apo-p7) was incubated with NOBA, a more random pattern of multiple S-S linkages was found. Oxidation of reconstituted p7 also occurred on treatment with cupric ions (Cu2+), and the same three major disulfide bonds were formed as in the reaction with NOBA. These results suggest the interpretation that the oxidation reaction occurs at the zinc-binding centers while zinc cations are still bound and that the two zinc fingers are not identical in their chemical properties. This latter point is consistent with the independent biological roles reported previously for the two fingers in the viral infection cycle.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009603 Nitroso Compounds Organic compounds containing the nitroso (-N Compounds, Nitroso
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D011489 Protein Denaturation Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002213 Capsid The outer protein protective shell of a virus, which protects the viral nucleic acid. Capsids are composed of repeating units (capsomers or capsomeres) of CAPSID PROTEINS which when assembled together form either an icosahedral or helical shape. Procapsid,Prohead,Capsids,Procapsids,Proheads
D003300 Copper A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55. Copper-63,Copper 63
D004220 Disulfides Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties. Disulfide
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000067856 Poly(ADP-ribose) Polymerase Inhibitors Chemicals and drugs that inhibit the action of POLY(ADP-RIBOSE)POLYMERASES. Inhibitors of Poly(ADP-ribose) Polymerase,PARP Inhibitor,Poly(ADP-Ribose) Polymerase Inhibitor,Poly(ADP-ribosylation) Inhibitor,Inhibitors of Poly(ADP-ribose) Polymerases,PARP Inhibitors,Poly(ADP-ribosylation) Inhibitors,Inhibitor, PARP,Inhibitors, PARP

Related Publications

X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
September 1998, Proceedings of the National Academy of Sciences of the United States of America,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
August 2003, Nucleic acids research,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
December 1996, Drug metabolism and disposition: the biological fate of chemicals,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
January 2004, Current topics in medicinal chemistry,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
June 2002, Proceedings of the National Academy of Sciences of the United States of America,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
June 2021, Viruses,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
June 1991, Biochemistry,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
February 2003, AIDS research and human retroviruses,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
April 1994, The EMBO journal,
X Yu, and Y Hathout, and C Fenselau, and R C Sowder, and L E Henderson, and W G Rice, and J Mendeleyev, and E Kun
December 2018, Chemistry (Weinheim an der Bergstrasse, Germany),
Copied contents to your clipboard!