Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein

D. Lee-Yoon, D. Easton, M. Murawski, Randy M Burd, J. R. Subjeck

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

A major mammalian heat shock protein of 110 kDa (hsp110) has long been observed, but has not been cloned. We have cloned the hamster cDNA for hsp110 and show that it hybridizes on a Northern blot to a 3.5-kilobase heat- inducible message in hamster and mouse. The hsp110 sequence was found to share an ~30-33% amino acid identity with members of the hsp70 family, most of which occurs in the conserved ATP-binding domain of these molecules. In addition, five sequences were found to be highly similar to hsp110. These are the sea urchin egg receptor for sperm (Foltz, K. R., Partin, J. S., and Lennarz, W. J. (1993) Science 259, 1421-1425) and additional sequences from human and Caenorhaditis elegans and two from yeast. The carboxyl-terminal two-thirds of hsp110 and these five related proteins contain a pattern of highly conserved regions of sequence unique to this group. A probe containing these conserved sequences was found to strongly cross-react on a Southern blot with genomic sequences from yeast to man. A Western blot analysis of several murine tissues indicates that hsp110 is constitutively expressed in all mouse tissues and is highly expressed in brain. Therefore, hsp110 belongs to a new category of large and structurally unique stress proteins that are the most distantly related known members of the hsp70 family.

Original languageEnglish (US)
Pages (from-to)15725-15733
Number of pages9
JournalJournal of Biological Chemistry
Volume270
Issue number26
DOIs
StatePublished - 1995
Externally publishedYes

Fingerprint

HSP110 Heat-Shock Proteins
Cloning
Organism Cloning
Proteins
Conserved Sequence
Cricetinae
Yeast
Yeasts
Tissue
Sea Urchins
Heat-Shock Proteins
Southern Blotting
Northern Blotting
Ovum
Brain
Complementary DNA
Hot Temperature
Adenosine Triphosphate
Western Blotting

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein. / Lee-Yoon, D.; Easton, D.; Murawski, M.; Burd, Randy M; Subjeck, J. R.

In: Journal of Biological Chemistry, Vol. 270, No. 26, 1995, p. 15725-15733.

Research output: Contribution to journalArticle

@article{b123a25bc4914503bf53165d23a0aebc,
title = "Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein",
abstract = "A major mammalian heat shock protein of 110 kDa (hsp110) has long been observed, but has not been cloned. We have cloned the hamster cDNA for hsp110 and show that it hybridizes on a Northern blot to a 3.5-kilobase heat- inducible message in hamster and mouse. The hsp110 sequence was found to share an ~30-33{\%} amino acid identity with members of the hsp70 family, most of which occurs in the conserved ATP-binding domain of these molecules. In addition, five sequences were found to be highly similar to hsp110. These are the sea urchin egg receptor for sperm (Foltz, K. R., Partin, J. S., and Lennarz, W. J. (1993) Science 259, 1421-1425) and additional sequences from human and Caenorhaditis elegans and two from yeast. The carboxyl-terminal two-thirds of hsp110 and these five related proteins contain a pattern of highly conserved regions of sequence unique to this group. A probe containing these conserved sequences was found to strongly cross-react on a Southern blot with genomic sequences from yeast to man. A Western blot analysis of several murine tissues indicates that hsp110 is constitutively expressed in all mouse tissues and is highly expressed in brain. Therefore, hsp110 belongs to a new category of large and structurally unique stress proteins that are the most distantly related known members of the hsp70 family.",
author = "D. Lee-Yoon and D. Easton and M. Murawski and Burd, {Randy M} and Subjeck, {J. R.}",
year = "1995",
doi = "10.1074/jbc.270.26.15725",
language = "English (US)",
volume = "270",
pages = "15725--15733",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "26",

}

TY - JOUR

T1 - Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein

AU - Lee-Yoon, D.

AU - Easton, D.

AU - Murawski, M.

AU - Burd, Randy M

AU - Subjeck, J. R.

PY - 1995

Y1 - 1995

N2 - A major mammalian heat shock protein of 110 kDa (hsp110) has long been observed, but has not been cloned. We have cloned the hamster cDNA for hsp110 and show that it hybridizes on a Northern blot to a 3.5-kilobase heat- inducible message in hamster and mouse. The hsp110 sequence was found to share an ~30-33% amino acid identity with members of the hsp70 family, most of which occurs in the conserved ATP-binding domain of these molecules. In addition, five sequences were found to be highly similar to hsp110. These are the sea urchin egg receptor for sperm (Foltz, K. R., Partin, J. S., and Lennarz, W. J. (1993) Science 259, 1421-1425) and additional sequences from human and Caenorhaditis elegans and two from yeast. The carboxyl-terminal two-thirds of hsp110 and these five related proteins contain a pattern of highly conserved regions of sequence unique to this group. A probe containing these conserved sequences was found to strongly cross-react on a Southern blot with genomic sequences from yeast to man. A Western blot analysis of several murine tissues indicates that hsp110 is constitutively expressed in all mouse tissues and is highly expressed in brain. Therefore, hsp110 belongs to a new category of large and structurally unique stress proteins that are the most distantly related known members of the hsp70 family.

AB - A major mammalian heat shock protein of 110 kDa (hsp110) has long been observed, but has not been cloned. We have cloned the hamster cDNA for hsp110 and show that it hybridizes on a Northern blot to a 3.5-kilobase heat- inducible message in hamster and mouse. The hsp110 sequence was found to share an ~30-33% amino acid identity with members of the hsp70 family, most of which occurs in the conserved ATP-binding domain of these molecules. In addition, five sequences were found to be highly similar to hsp110. These are the sea urchin egg receptor for sperm (Foltz, K. R., Partin, J. S., and Lennarz, W. J. (1993) Science 259, 1421-1425) and additional sequences from human and Caenorhaditis elegans and two from yeast. The carboxyl-terminal two-thirds of hsp110 and these five related proteins contain a pattern of highly conserved regions of sequence unique to this group. A probe containing these conserved sequences was found to strongly cross-react on a Southern blot with genomic sequences from yeast to man. A Western blot analysis of several murine tissues indicates that hsp110 is constitutively expressed in all mouse tissues and is highly expressed in brain. Therefore, hsp110 belongs to a new category of large and structurally unique stress proteins that are the most distantly related known members of the hsp70 family.

UR - http://www.scopus.com/inward/record.url?scp=0029079045&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029079045&partnerID=8YFLogxK

U2 - 10.1074/jbc.270.26.15725

DO - 10.1074/jbc.270.26.15725

M3 - Article

C2 - 7797574

AN - SCOPUS:0029079045

VL - 270

SP - 15725

EP - 15733

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 26

ER -