Characterization of mouse Clpp protease cDNA, gene, and protein.

B S Andresen; T J Corydon; M Wilsbech; P Bross; T F Hindkjaer; L Bolund; N Gregersen; L D Schroeder

Characterization of mouse Clpp protease cDNA, gene, and protein.

B S Andresen, T J Corydon, M Wilsbech, P Bross, T F Hindkjaer, L Bolund, N Gregersen, L D Schroeder

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

5 Citations (Scopus)

Abstract

Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins. In the present study, we have characterized the mouse Clpp cDNA sequence, the organization of the mouse gene, the chromosomal localization, and the tissue-specific expression pattern. Moreover. the cellular localization and processing of mouse Clpp was studied by overexpression in transfected eukaryotic cells. Our results indicate that mouse and human Clpp have similar roles, and they provide the molecular basis for establishing a Clpp knockout mouse and to study its phenotype, thereby shedding light on a possible role of Clpp in human disease.

Original language	English
Journal	Mammalian Genome
Volume	11
Issue	4
Pages (from-to)	275-80
Number of pages	5
ISSN	0938-8990
Publication status	Published - 2000

Keywords

Adenosine Triphosphatases
Animals
Base Sequence
Chromosome Mapping
DNA Primers
DNA, Complementary
Endopeptidase Clp
Exons
Humans
Introns
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Recombinant Proteins
Serine Endopeptidases

Cite this

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title = "Characterization of mouse Clpp protease cDNA, gene, and protein.",

abstract = "Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins. In the present study, we have characterized the mouse Clpp cDNA sequence, the organization of the mouse gene, the chromosomal localization, and the tissue-specific expression pattern. Moreover. the cellular localization and processing of mouse Clpp was studied by overexpression in transfected eukaryotic cells. Our results indicate that mouse and human Clpp have similar roles, and they provide the molecular basis for establishing a Clpp knockout mouse and to study its phenotype, thereby shedding light on a possible role of Clpp in human disease.",

keywords = "Adenosine Triphosphatases, Animals, Base Sequence, Chromosome Mapping, DNA Primers, DNA, Complementary, Endopeptidase Clp, Exons, Humans, Introns, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Recombinant Proteins, Serine Endopeptidases",

author = "Andresen, {B S} and Corydon, {T J} and M Wilsbech and P Bross and Hindkjaer, {T F} and L Bolund and N Gregersen and Schroeder, {L D}",

year = "2000",

language = "English",

volume = "11",

pages = "275--80",

journal = "Mammalian Genome",

issn = "0938-8990",

publisher = "Springer",

number = "4",

}

TY - JOUR

T1 - Characterization of mouse Clpp protease cDNA, gene, and protein.

AU - Andresen, B S

AU - Corydon, T J

AU - Wilsbech, M

AU - Bross, P

AU - Hindkjaer, T F

AU - Bolund, L

AU - Gregersen, N

AU - Schroeder, L D

PY - 2000

Y1 - 2000

N2 - Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins. In the present study, we have characterized the mouse Clpp cDNA sequence, the organization of the mouse gene, the chromosomal localization, and the tissue-specific expression pattern. Moreover. the cellular localization and processing of mouse Clpp was studied by overexpression in transfected eukaryotic cells. Our results indicate that mouse and human Clpp have similar roles, and they provide the molecular basis for establishing a Clpp knockout mouse and to study its phenotype, thereby shedding light on a possible role of Clpp in human disease.

AB - Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins. In the present study, we have characterized the mouse Clpp cDNA sequence, the organization of the mouse gene, the chromosomal localization, and the tissue-specific expression pattern. Moreover. the cellular localization and processing of mouse Clpp was studied by overexpression in transfected eukaryotic cells. Our results indicate that mouse and human Clpp have similar roles, and they provide the molecular basis for establishing a Clpp knockout mouse and to study its phenotype, thereby shedding light on a possible role of Clpp in human disease.

KW - Adenosine Triphosphatases

KW - Animals

KW - Base Sequence

KW - Chromosome Mapping

KW - DNA Primers

KW - DNA, Complementary

KW - Endopeptidase Clp

KW - Exons

KW - Humans

KW - Introns

KW - Mice

KW - Mice, Inbred C57BL

KW - Molecular Sequence Data

KW - Recombinant Proteins

KW - Serine Endopeptidases

M3 - Journal article

C2 - 10754102

SN - 0938-8990

VL - 11

SP - 275

EP - 280

JO - Mammalian Genome

JF - Mammalian Genome

IS - 4

ER -

Characterization of mouse Clpp protease cDNA, gene, and protein.

Abstract

Keywords

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