Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein

R. S. Pillai; C. L. Will; R. Lührmann; D. Schümperli; Berndt Marino Muller

doi:10.1093/emboj/20.19.5470

Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein

R. S. Pillai, C. L. Will, R. Lührmann, D. Schümperli, Berndt Marino Muller

Medical Sciences

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

135 Citations (Scopus)

Abstract

U7 snRNPs; were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies of the cell nucleus. Its incorporation into U7 snRNPs; is largely dictated by the special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.

Original language	English
Pages (from-to)	5470-5479
Number of pages	9
Journal	EMBO Journal
Volume	20
Issue number	19
DOIs	https://doi.org/10.1093/emboj/20.19.5470
Publication status	Published - Oct 2001

Keywords

Cajal
coiled bodies
histone pre-mRNA 3 ' processing
Sm core structure
Sm-like protein
small nuclear ribonucleoprotein
PRE-MESSENGER-RNA
SMALL NUCLEAR-RNA
COILED BODIES
U6 SNRNA
RIBONUCLEOPROTEIN-PARTICLES
SPLICEOSOMAL SNRNPS
STRUCTURAL DOMAIN
BINDING-SITE
IN-VITRO
IDENTIFICATION

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@article{2951d653f0284021909a8eef81d4aa67,

title = "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein",

abstract = "U7 snRNPs; were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies of the cell nucleus. Its incorporation into U7 snRNPs; is largely dictated by the special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.",

keywords = "Cajal, coiled bodies, histone pre-mRNA 3 ' processing, Sm core structure, Sm-like protein, small nuclear ribonucleoprotein, PRE-MESSENGER-RNA, SMALL NUCLEAR-RNA, COILED BODIES, U6 SNRNA, RIBONUCLEOPROTEIN-PARTICLES, SPLICEOSOMAL SNRNPS, STRUCTURAL DOMAIN, BINDING-SITE, IN-VITRO, IDENTIFICATION",

author = "Pillai, {R. S.} and Will, {C. L.} and R. L{\"u}hrmann and D. Sch{\"u}mperli and Muller, {Berndt Marino}",

year = "2001",

month = oct,

doi = "10.1093/emboj/20.19.5470",

language = "English",

volume = "20",

pages = "5470--5479",

journal = "EMBO Journal",

issn = "0261-4189",

publisher = "Nature Publishing Group",

number = "19",

}

TY - JOUR

T1 - Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein

AU - Pillai, R. S.

AU - Will, C. L.

AU - Lührmann, R.

AU - Schümperli, D.

AU - Muller, Berndt Marino

PY - 2001/10

Y1 - 2001/10

N2 - U7 snRNPs; were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies of the cell nucleus. Its incorporation into U7 snRNPs; is largely dictated by the special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.

AB - U7 snRNPs; were isolated from HeLa cells by biochemical fractionation, followed by affinity purification with a biotinylated oligonucleotide complementary to U7 snRNA. Purified U7 snRNPs lack the Sm proteins D1 and D2, but contain additional polypeptides of 14, 50 and 70 kDa. Microsequencing identified the 14 kDa polypeptide as a new Sm-like protein related to Sm D1 and D3. Like U7 snRNA, this protein, named Lsm10, is enriched in Cajal bodies of the cell nucleus. Its incorporation into U7 snRNPs; is largely dictated by the special Sm binding site of U7 snRNA. This novel type of Sm complex, composed of both conventional Sm proteins and the Sm-like Lsm10, is most likely to be important for U7 snRNP function and subcellular localization.

KW - Cajal

KW - coiled bodies

KW - histone pre-mRNA 3 ' processing

KW - Sm core structure

KW - Sm-like protein

KW - small nuclear ribonucleoprotein

KW - PRE-MESSENGER-RNA

KW - SMALL NUCLEAR-RNA

KW - COILED BODIES

KW - U6 SNRNA

KW - RIBONUCLEOPROTEIN-PARTICLES

KW - SPLICEOSOMAL SNRNPS

KW - STRUCTURAL DOMAIN

KW - BINDING-SITE

KW - IN-VITRO

KW - IDENTIFICATION

U2 - 10.1093/emboj/20.19.5470

DO - 10.1093/emboj/20.19.5470

M3 - Article

SN - 0261-4189

VL - 20

SP - 5470

EP - 5479

JO - EMBO Journal

JF - EMBO Journal

IS - 19

ER -

Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein

Abstract

Keywords

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