Structure and function of archaeal box C/D sRNP core proteins

Mohamed Aittaleb; Rumana Rashid; Qiong Chen; John R. Palmer; Charles J. Daniels; Hong Li

doi:10.1038/nsb905

Structure and function of archaeal box C/D sRNP core proteins

Mohamed Aittaleb
, Rumana Rashid
, Qiong Chen
, John R. Palmer
, Charles J. Daniels
, Hong Li^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

115 Citations (Scopus)

Abstract

Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin-Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.

Original language	English
Pages (from-to)	256-263
Number of pages	8
Journal	Nature Structural Biology
Volume	10
Issue number	4
DOIs	https://doi.org/10.1038/nsb905
Publication status	Published - 1 Apr 2003
Externally published	Yes

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title = "Structure and function of archaeal box C/D sRNP core proteins",

abstract = "Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 {\AA} resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin-Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.",

author = "Mohamed Aittaleb and Rumana Rashid and Qiong Chen and Palmer, \{John R.\} and Daniels, \{Charles J.\} and Hong Li",

year = "2003",

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doi = "10.1038/nsb905",

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TY - JOUR

T1 - Structure and function of archaeal box C/D sRNP core proteins

AU - Aittaleb, Mohamed

AU - Rashid, Rumana

AU - Chen, Qiong

AU - Palmer, John R.

AU - Daniels, Charles J.

AU - Li, Hong

PY - 2003/4/1

Y1 - 2003/4/1

N2 - Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin-Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.

AB - Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin-Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.

UR - https://www.scopus.com/pages/publications/0037389971

U2 - 10.1038/nsb905

DO - 10.1038/nsb905

M3 - Article

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AN - SCOPUS:0037389971

SN - 1072-8368

VL - 10

SP - 256

EP - 263

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 4

ER -

Structure and function of archaeal box C/D sRNP core proteins

Abstract

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