Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G

Kuan Ming Chen; Natalia Martemyanova; Yongjian Lu; Keisuke Shindo; Hiroshi Matsuo; Reuben S. Harris

doi:10.1016/j.febslet.2007.08.076

Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G

Kuan Ming Chen, Natalia Martemyanova, Yongjian Lu, Keisuke Shindo, Hiroshi Matsuo, Reuben S. Harris

Producción científica: Article › revisión exhaustiva

44 Citas (Scopus)

Resumen

APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.

Idioma original	English (US)
Páginas (desde-hasta)	4761-4766
Número de páginas	6
Publicación	FEBS Letters
Volumen	581
N.º	24
DOI	https://doi.org/10.1016/j.febslet.2007.08.076
Estado	Published - oct 2 2007
Publicado de forma externa	Sí

ASJC Scopus subject areas

Genetics
Molecular Biology
Biophysics
Structural Biology
Biochemistry
Cell Biology

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title = "Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G",

abstract = "APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.",

keywords = "APOBEC3G, DNA cytosine deamination, DNA editing, Hypermutation",

author = "Chen, {Kuan Ming} and Natalia Martemyanova and Yongjian Lu and Keisuke Shindo and Hiroshi Matsuo and Harris, {Reuben S.}",

note = "Funding Information: This work was supported by NIH Grants AI064046 (RSH) and AI073167 (HM) and by the University of Minnesota{\textquoteright}s Leukemia Research Fund (RSH) and Grant-in-Aid Program (HM). R.S.H. is a Searle Scholar and a University of Minnesota McKnight Land Grant Assistant Professor. We thank A. Briggs, P. Gross and Y. Sham for technical assistance, Harris and Matsuo laboratory members for helpful discussions and the University of Minnesota AGAC and SCI for DNA sequencing and computational resources, respectively. ",

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AU - Chen, Kuan Ming

AU - Martemyanova, Natalia

AU - Lu, Yongjian

AU - Shindo, Keisuke

AU - Matsuo, Hiroshi

AU - Harris, Reuben S.

N1 - Funding Information: This work was supported by NIH Grants AI064046 (RSH) and AI073167 (HM) and by the University of Minnesota’s Leukemia Research Fund (RSH) and Grant-in-Aid Program (HM). R.S.H. is a Searle Scholar and a University of Minnesota McKnight Land Grant Assistant Professor. We thank A. Briggs, P. Gross and Y. Sham for technical assistance, Harris and Matsuo laboratory members for helpful discussions and the University of Minnesota AGAC and SCI for DNA sequencing and computational resources, respectively.

PY - 2007/10/2

Y1 - 2007/10/2

N2 - APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.

AB - APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.

KW - APOBEC3G

KW - DNA cytosine deamination

KW - DNA editing

KW - Hypermutation

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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G

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