Structure and real-time monitoring of the enzymatic reaction of APOBEC3G which is involved in anti-HIV activity.
Human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G) is known to play a role in intrinsic cellular immunity against human immunodeficiency virus type 1 (HIV-1). The antiretroviral activity of APOBEC3G is associated with hypermutation of viral DNA through cytidine deamination. APOBEC3G contains two cytidine deaminase domains that are characterized by a highly conserved zinc-coordinating motif. It is known that only the C-terminal domain of APOBEC3G (c-APOBEC3G) is involved in the catalytic activity. Here, we present the solution structure and the interaction with single-stranded DNA of c-APOBEC3G. Furthermore, we have succeeded for the first time in monitoring the deamination reaction of c-APOBEC3G in real-time using NMR signals. The monitoring has demonstrated that the deamination reaction occurs in a strict 3'-->5'
Furukawa
Ayako
A
Department of Supramolecular Biology, Graduate School of Nanobioscience, Yokohama City University, Yokohama 230-0045, Japan.
Nagata
Takashi
T
Matsugami
Akimasa
A
Habu
Yuichirou
Y
Sugiyama
Ryuichi
R
Hayashi
Fumiaki
F
Kobayashi
Naohiro
N
Yokoyama
Shigeyuki
S
Takaku
Hiroshi
H
Katahira
Masato
M
D000071480:APOBEC-3G Deaminase; D003564:Cytidine Deaminase / Q000737:chemistry*; D004277:DNA, Single-Stranded / Q000737:chemistry*; D015497:HIV-1 / Q000235:genetics; D006801:Humans; D007700:Kinetics; D019906:Nuclear Magnetic Resonance, Biomolecular
D004277:DNA, Single-Stranded; D000071480:APOBEC-3G Deaminase; C464924:APOBEC3G protein, human; D003564:Cytidine Deaminase