Maturation and intranuclear transport of pre-ribosomes requires Noc proteins

P  Milkereit; O  Gadal; A  Podtelejnikov; S  Trumtel; N  Gas; E  Petfalski; D  Tollervey; M  Mann; E  Hurt; H  Tschochner

Maturation and intranuclear transport of pre-ribosomes requires Noc proteins

P Milkereit, O Gadal, A Podtelejnikov, S Trumtel, N Gas, E Petfalski, D Tollervey, M Mann, E Hurt, H Tschochner

School of Biological Sciences

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

Abstract / Description of output

How pre-ribosomes temporally and spatially mature during intranuclear biogenesis is not known. Here, we report three nucleolar proteins, Noc1p to Noc3p, that are required for ribosome maturation and transport. They can be isolated in two distinct complexes: Noc1p/Noc2p associates with 90S and 66S pre-ribosomes and is enriched in the nucleolus, and Noc2p/Noc3p associates with 66S pre-ribosomes and is mainly nucleoplasmic. Mutation of each Noc protein impairs intranuclear transport of 60S subunits at different stages and inhibits pre-rRNA processing. Overexpression of a conserved domain common to Noc1p and Noc3p is dominant-negative for cell growth, with a defect int nuclear 60S subunit transport, but no inhibition of pre-RNA processing. We propose that the dynamic interaction of Noc proteins is crucial for intranuclear movement of ribosomal precursor particles, and, thereby represent a prerequisite for proper maturation.

Original language	English
Pages (from-to)	499-509
Number of pages	11
Journal	Cell
Volume	105
Issue number	4
Publication status	Published - 18 May 2001

Cite this

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title = "Maturation and intranuclear transport of pre-ribosomes requires Noc proteins",

abstract = "How pre-ribosomes temporally and spatially mature during intranuclear biogenesis is not known. Here, we report three nucleolar proteins, Noc1p to Noc3p, that are required for ribosome maturation and transport. They can be isolated in two distinct complexes: Noc1p/Noc2p associates with 90S and 66S pre-ribosomes and is enriched in the nucleolus, and Noc2p/Noc3p associates with 66S pre-ribosomes and is mainly nucleoplasmic. Mutation of each Noc protein impairs intranuclear transport of 60S subunits at different stages and inhibits pre-rRNA processing. Overexpression of a conserved domain common to Noc1p and Noc3p is dominant-negative for cell growth, with a defect int nuclear 60S subunit transport, but no inhibition of pre-RNA processing. We propose that the dynamic interaction of Noc proteins is crucial for intranuclear movement of ribosomal precursor particles, and, thereby represent a prerequisite for proper maturation.",

author = "P Milkereit and O Gadal and A Podtelejnikov and S Trumtel and N Gas and E Petfalski and D Tollervey and M Mann and E Hurt and H Tschochner",

year = "2001",

month = may,

day = "18",

language = "English",

volume = "105",

pages = "499--509",

journal = "Cell",

issn = "0092-8674",

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TY - JOUR

T1 - Maturation and intranuclear transport of pre-ribosomes requires Noc proteins

AU - Milkereit, P

AU - Gadal, O

AU - Podtelejnikov, A

AU - Trumtel, S

AU - Gas, N

AU - Petfalski, E

AU - Tollervey, D

AU - Mann, M

AU - Hurt, E

AU - Tschochner, H

PY - 2001/5/18

Y1 - 2001/5/18

N2 - How pre-ribosomes temporally and spatially mature during intranuclear biogenesis is not known. Here, we report three nucleolar proteins, Noc1p to Noc3p, that are required for ribosome maturation and transport. They can be isolated in two distinct complexes: Noc1p/Noc2p associates with 90S and 66S pre-ribosomes and is enriched in the nucleolus, and Noc2p/Noc3p associates with 66S pre-ribosomes and is mainly nucleoplasmic. Mutation of each Noc protein impairs intranuclear transport of 60S subunits at different stages and inhibits pre-rRNA processing. Overexpression of a conserved domain common to Noc1p and Noc3p is dominant-negative for cell growth, with a defect int nuclear 60S subunit transport, but no inhibition of pre-RNA processing. We propose that the dynamic interaction of Noc proteins is crucial for intranuclear movement of ribosomal precursor particles, and, thereby represent a prerequisite for proper maturation.

AB - How pre-ribosomes temporally and spatially mature during intranuclear biogenesis is not known. Here, we report three nucleolar proteins, Noc1p to Noc3p, that are required for ribosome maturation and transport. They can be isolated in two distinct complexes: Noc1p/Noc2p associates with 90S and 66S pre-ribosomes and is enriched in the nucleolus, and Noc2p/Noc3p associates with 66S pre-ribosomes and is mainly nucleoplasmic. Mutation of each Noc protein impairs intranuclear transport of 60S subunits at different stages and inhibits pre-rRNA processing. Overexpression of a conserved domain common to Noc1p and Noc3p is dominant-negative for cell growth, with a defect int nuclear 60S subunit transport, but no inhibition of pre-RNA processing. We propose that the dynamic interaction of Noc proteins is crucial for intranuclear movement of ribosomal precursor particles, and, thereby represent a prerequisite for proper maturation.

M3 - Article

SN - 0092-8674

VL - 105

SP - 499

EP - 509

JO - Cell

JF - Cell

IS - 4

ER -

Maturation and intranuclear transport of pre-ribosomes requires Noc proteins

Abstract / Description of output

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