核糖核酸酶Ⅲ

現有可用的蛋白結構：
Pfam	結構（舊版） / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum（英語：PDBsum）	結構概要
PDB	1o0wB:51-141 2a11A:41-134 1jfzA:37-121 1rc7A:37-121 1yywA:37-121 1i4sA:37-121 1rc5B:37-121 1yyoA:37-121 1yykB:37-121 1yz9A:37-121 2fflA:333-418 1u61A:10-111

核糖核酸酶Ⅲ
核糖核酸酶Ⅲ
	RNA酶III與雙股RNA的交互作用
鑑定
標誌	RNA酶III
Pfam	PF00636（舊版）
InterPro（英語：InterPro）	IPR000999
PROSITE（英語：PROSITE）	PDOC00448
SCOP（英語：Structural Classification of Proteins）	1jfz / SUPFAM
Pfam
現有可用的蛋白結構：
Pfam	結構（舊版） / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum（英語：PDBsum）	結構概要
PDB	1o0wB:51-141 2a11A:41-134 1jfzA:37-121 1rc7A:37-121 1yywA:37-121 1i4sA:37-121 1rc5B:37-121 1yyoA:37-121 1yykB:37-121 1yz9A:37-121 2fflA:333-418 1u61A:10-111

RNA酶III（Ribonuclease III，簡稱RNase III或RNase C^[1]，BRENDA（英語：BRENDA）編號：3.1.26.3 （頁面存檔備份，存於網際網路檔案館））為一類RNA酶，屬切割雙股RNA的內切酶，均具有RNA酶III結構域^[2]。此類RNA酶參與rRNA、SnRNA、SnoRNA與miRNA等RNA的生成過程^[3]，可在細胞中的特定位置切割這些RNA的前驅物以產生成熟的RNA^[4]^[5]。三域生物與部分病毒皆具有RNA酶III。

RNA酶III可依結構域分為四型^[6]。切割miRNA前驅物的Drosha與Dicer分別屬於三型與四型的RNA酶III^[7]^[8]

參考文獻

^ Filippov, Valery; Solovyev, Victor; Filippova, Maria; Gill, Sarjeet S. A novel type of RNase III family proteins in eukaryotes. Gene. 7 March 2000, 245 (1): 213–221. PMID 10713462. doi:10.1016/S0378-1119(99)00571-5.
^ Conrad, Christian; Rauhut, Reinhard. Ribonuclease III: new sense from nuisance. The International Journal of Biochemistry & Cell Biology. February 2002, 34 (2): 116–129. PMID 11809414. doi:10.1016/S1357-2725(01)00112-1.
^ Zamore, Phollip D. Thirty-Three Years Later, a Glimpse at the Ribonuclease III Active Site. Molecular Cell. December 2001, 8 (6): 1158–1160. PMID 11885596. doi:10.1016/S1097-2765(01)00418-X .
^ Inada, T.; Nakamura, Y. Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli. Biochimie. 1995, 77 (4): 294–302. PMID 8589060. doi:10.1016/0300-9084(96)88139-9.
^ Park, Hongmarn; Yakhnin, Helen; Connolly, Michael; Romeo, Tony; Babitzke, Paul; Gourse, R. L. CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of Transcripts That Have Been Previously Processed by RNase III and PNPase. Journal of Bacteriology. 15 December 2015, 197 (24): 3751–3759. PMC 4652041 . PMID 26438818. doi:10.1128/JB.00721-15.
^ Liang YH, Lavoie M, Comeau MA, Abou Elela S, Ji X. Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection.. Mol Cell. 2014, 54 (3): 431–44. PMC 4019767 . PMID 24703949. doi:10.1016/j.molcel.2014.03.006.
^ Filippov V, Solovyev V, Filippova M, Gill SS. A novel type of RNase III family proteins in eukaryotes. Gene. Mar 2000, 245 (1): 213–221. PMID 10713462. doi:10.1016/S0378-1119(99)00571-5.
^ Bernstein E, Caudy AA, Hammond SM, Hannon GJ. Role for a bidentate ribonuclease in the initiation step of RNA interference.. Nature. 2001, 409 (6818): 363–6. PMID 11201747. doi:10.1038/35053110.

[1] Filippov, Valery; Solovyev, Victor; Filippova, Maria; Gill, Sarjeet S. A novel type of RNase III family proteins in eukaryotes. Gene. 7 March 2000, 245 (1): 213–221. PMID 10713462. doi:10.1016/S0378-1119(99)00571-5.

[2] Conrad, Christian; Rauhut, Reinhard. Ribonuclease III: new sense from nuisance. The International Journal of Biochemistry & Cell Biology. February 2002, 34 (2): 116–129. PMID 11809414. doi:10.1016/S1357-2725(01)00112-1.

[3] Zamore, Phollip D. Thirty-Three Years Later, a Glimpse at the Ribonuclease III Active Site. Molecular Cell. December 2001, 8 (6): 1158–1160. PMID 11885596. doi:10.1016/S1097-2765(01)00418-X .

[4] Inada, T.; Nakamura, Y. Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli. Biochimie. 1995, 77 (4): 294–302. PMID 8589060. doi:10.1016/0300-9084(96)88139-9.

[pnp_Reg-5] Park, Hongmarn; Yakhnin, Helen; Connolly, Michael; Romeo, Tony; Babitzke, Paul; Gourse, R. L. CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of Transcripts That Have Been Previously Processed by RNase III and PNPase. Journal of Bacteriology. 15 December 2015, 197 (24): 3751–3759. PMC 4652041 . PMID 26438818. doi:10.1128/JB.00721-15.

[pmid24703949-6] Liang YH, Lavoie M, Comeau MA, Abou Elela S, Ji X. Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler mechanism for substrate selection.. Mol Cell. 2014, 54 (3): 431–44. PMC 4019767 . PMID 24703949. doi:10.1016/j.molcel.2014.03.006.

[pmid10713462-7] Filippov V, Solovyev V, Filippova M, Gill SS. A novel type of RNase III family proteins in eukaryotes. Gene. Mar 2000, 245 (1): 213–221. PMID 10713462. doi:10.1016/S0378-1119(99)00571-5.

[pmid11201747-8] Bernstein E, Caudy AA, Hammond SM, Hannon GJ. Role for a bidentate ribonuclease in the initiation step of RNA interference.. Nature. 2001, 409 (6818): 363–6. PMID 11201747. doi:10.1038/35053110.

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