Spatial proximity of the HIV-1 nucleocapsid protein zinc fingers investigated by time-resolved fluorescence and fluorescence resonance energy transfer.

Important note: Information in this article was accurate in 1995. The state of the art may have changed since the publication date.

Spatial proximity of the HIV-1 nucleocapsid protein zinc fingers investigated by time-resolved fluorescence and fluorescence resonance energy transfer.

Biochemistry. 1994 Oct 11;33(40):12085-91. Unique Identifier : AIDSLINE MED/95001923
Mely Y; Jullian N; Morellet N; De Rocquigny H; Dong CZ; Piemont E; Roques BP; Gerard D; Laboratoire de Biophysique de la Faculte de Pharmacie, CNRS UA; 491, Universite Louis Pasteur, Strasbourg, Illkirch, France.

Abstract: The three-dimensional structure of peptides encompassing the two zinc-saturated finger motifs of the nucleocapsid protein NCp7 of HIV-1 has been reported by several groups. Whereas the folded structures of the finger motifs were in good agreement, discrepancies existed concerning their spatial relationship since the fingers were found either close to each other [Morellet, N., Jullian, N., De Rocquigny, H., Maigret, B., Darlix, J. L., & Roques, B. P. (1992) Embo J. 11, 3059-3065] or independently folded [Omichinski, J. G., Clore, G. M., Sakaguchi, K., Appella, E., & Gronenborn, A. M. (1991) FEBS Lett. 292, 25-30, Summers, M. F., Henderson, L. E., Chance, M. R., Bess, J. W., Jr., South, T. L., Blake, P. R., Sagi, I., Perez-Alvarado, G., Sowder, R.C., III, Hare, D.R., & Arthur, L. O. (1992) Protein Sci. 1, 563-574]. As in the interacting finger model, Phe16 in the NH2-terminal finger and Trp37 in the COOH-terminal finger were found to be spatially close, the fluorescence properties of the aromatic residues at positions 16 and 37 in the wild-type and two conservatively substituted (12-53) NCp7 peptides were investigated and compared with those of three negative control derivatives where the finger motifs were not in close contact. Direct distance measurements by Tyr-Trp fluorescence resonance energy transfer of the former derivatives yielded a 7-12 A interchromophore distance range which is clearly inconsistent with the 12.5-18 A range measured for the negative controls and thus a random orientation of the zinc finger motifs.(ABSTRACT TRUNCATED AT 250 WORDS)

Keywords: Algorithms Amino Acid Sequence Anisotropy Capsid/*CHEMISTRY/ULTRASTRUCTURE Gene Products, gag/*CHEMISTRY/ULTRASTRUCTURE Human Molecular Sequence Data Nuclear Magnetic Resonance Protein Conformation Spectrometry, Fluorescence Support, Non-U.S. Gov't Tryptophan/CHEMISTRY/GENETICS *Zinc Fingers/GENETICS JOURNAL ARTICLE
950130
M9510808

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