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Titolo:
Crystal structure of archaeal RNase HII: a homologue of human major RNase H
Autore:
Lai, LH; Yokota, H; Hung, LW; Kim, R; Kim, SH;
Indirizzi:
Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 pt Chem, Berkeley, CA 94720 USA Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 ley Lab, Berkeley, CA 94720 USA Peking Univ, Coll Chem, Beijing 100871, Peoples R China Peking Univ Beijing Peoples R China 100871 ijing 100871, Peoples R China Peking Univ, Inst Chem Phys, Beijing 100871, Peoples R China Peking Univ Beijing Peoples R China 100871 ijing 100871, Peoples R China
Titolo Testata:
STRUCTURE WITH FOLDING & DESIGN
fascicolo: 8, volume: 8, anno: 2000,
pagine: 897 - 904
SICI:
0969-2126(20000815)8:8<897:CSOARH>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI RIBONUCLEASE HI; SARCOMA VIRUS INTEGRASE; ELECTRON-DENSITY MAPS; ESCHERICHIA-COLI; MACROMOLECULAR STRUCTURES; REVERSE-TRANSCRIPTASE; CATALYTIC DOMAIN; RNHB GENE; DNA; IDENTIFICATION;
Keywords:
archaeal RNase H; DNA replication; removal of Okazaki fragment; RNase H;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Kim, SH Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 Berkeley, CA 94720 USA
Citazione:
L.H. Lai et al., "Crystal structure of archaeal RNase HII: a homologue of human major RNase H", STRUCT F D, 8(8), 2000, pp. 897-904

Abstract

Background: RNases H are present in all organisms and cleave RNAs in RNA/DNA hybrids. There are two major types of RNases H that have little similarity in sequence, size and specificity. The structure of RNase HI, the smaller enzyme and most abundant in bacteria, has been extensively studied. However, no structural information is available for the larger RNase H, which ismost abundant in eukaryotes and archaea. Mammalian RNase H participates inDNA replication, removal of the Okazaki fragments and possibly DNA repair. Results: The crystal structure of RNase HII from the hypothermophile Methanococcus jannaschii, which is homologous to mammalian RNase H, was solved using a multiwavelength anomalous dispersion (MAD) phasing method at 2 Angstrom resolution. The structure contains two compact domains. Despite the absence of sequence similarity, the large N-terminal domain shares a similar fold with the RNase HI of bacteria. The active site of RNase HII contains three aspartates: Asp7, Asp112 and Asp149. The nucleotide-binding site is located in the cleft between the N-terminal and C-terminal domains. Conclusions: Despite a lack of any detectable similarity in primary structure, RNase HII shares a similar structural domain with RNase HI, suggestingthat the two classes of RNases H have a common catalytic mechanism and possibly a common evolutionary origin. The involvement of the unique C-terminal domain in substrate recognition explains the different reaction specificity observed between the two classes of RNase H.

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Documento generato il 04/07/20 alle ore 18:31:53