The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous

George N. DeMartino, Kim Orth, Marci L. McCullough, Lawrence W. Lee, Terry Z. Munn, Carolyn R. Moomaw, Paul A. Dawson, Clive A. Slaughter

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Macropain (proteasome) is a high-molecular-weight proteinase complex composed of at least 13 electrophoretically distinct subunits. Previous work, including peptide mapping and limited amino acid sequencing, suggested that most of the subunits belong to an evolutionarily related group of different gene products (Lee et al. (1990) Biochim. Biophys. Acta. 1037, 178-185). In order to define the extent and pattern of subunit relatedness, and to determine the structural basis for possible similarities and differences in subunit functions, we are deducing the primary structures of macropain subunits by cDNA cloning and DNA sequence analysis. We report here the primary structures of four subunits. The data clearly demonstrate that the proteins represent different, but homologous gene products. Surprisingly, no evidence for homology with any other protein, including proteinases, was obtained. These results suggest that macropain is comprised of a previously unidentified family of evolutionarily related polypeptides. Because biochemical data indicate that macropain contains several different proteinase activities, the current results raise the possibility that the macropain complex is composed of a group of novel proteinases, distinct from those of other structurally identifiable proteinase families.

Original languageEnglish (US)
Pages (from-to)29-38
Number of pages10
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1079
Issue number1
DOIs
StatePublished - Aug 9 1991
Externally publishedYes

Fingerprint

Proteasome Endopeptidase Complex
Peptide Hydrolases
Molecular Weight
Molecular weight
Genes
Peptides
Peptide Mapping
Cloning
DNA sequences
Protein Sequence Analysis
DNA Sequence Analysis
Organism Cloning
Proteins
Complementary DNA
Amino Acids

Keywords

  • Macropain
  • Multicatalytic proteinase
  • Proteasome
  • Ubiquitin

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. / DeMartino, George N.; Orth, Kim; McCullough, Marci L.; Lee, Lawrence W.; Munn, Terry Z.; Moomaw, Carolyn R.; Dawson, Paul A.; Slaughter, Clive A.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1079, No. 1, 09.08.1991, p. 29-38.

Research output: Contribution to journalArticle

DeMartino, George N. ; Orth, Kim ; McCullough, Marci L. ; Lee, Lawrence W. ; Munn, Terry Z. ; Moomaw, Carolyn R. ; Dawson, Paul A. ; Slaughter, Clive A. / The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1991 ; Vol. 1079, No. 1. pp. 29-38.
@article{e28aa48d2ac14e9a946bd6903224098d,
title = "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous",
abstract = "Macropain (proteasome) is a high-molecular-weight proteinase complex composed of at least 13 electrophoretically distinct subunits. Previous work, including peptide mapping and limited amino acid sequencing, suggested that most of the subunits belong to an evolutionarily related group of different gene products (Lee et al. (1990) Biochim. Biophys. Acta. 1037, 178-185). In order to define the extent and pattern of subunit relatedness, and to determine the structural basis for possible similarities and differences in subunit functions, we are deducing the primary structures of macropain subunits by cDNA cloning and DNA sequence analysis. We report here the primary structures of four subunits. The data clearly demonstrate that the proteins represent different, but homologous gene products. Surprisingly, no evidence for homology with any other protein, including proteinases, was obtained. These results suggest that macropain is comprised of a previously unidentified family of evolutionarily related polypeptides. Because biochemical data indicate that macropain contains several different proteinase activities, the current results raise the possibility that the macropain complex is composed of a group of novel proteinases, distinct from those of other structurally identifiable proteinase families.",
keywords = "Macropain, Multicatalytic proteinase, Proteasome, Ubiquitin",
author = "DeMartino, {George N.} and Kim Orth and McCullough, {Marci L.} and Lee, {Lawrence W.} and Munn, {Terry Z.} and Moomaw, {Carolyn R.} and Dawson, {Paul A.} and Slaughter, {Clive A.}",
year = "1991",
month = "8",
day = "9",
doi = "10.1016/0167-4838(91)90020-Z",
language = "English (US)",
volume = "1079",
pages = "29--38",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous

AU - DeMartino, George N.

AU - Orth, Kim

AU - McCullough, Marci L.

AU - Lee, Lawrence W.

AU - Munn, Terry Z.

AU - Moomaw, Carolyn R.

AU - Dawson, Paul A.

AU - Slaughter, Clive A.

PY - 1991/8/9

Y1 - 1991/8/9

N2 - Macropain (proteasome) is a high-molecular-weight proteinase complex composed of at least 13 electrophoretically distinct subunits. Previous work, including peptide mapping and limited amino acid sequencing, suggested that most of the subunits belong to an evolutionarily related group of different gene products (Lee et al. (1990) Biochim. Biophys. Acta. 1037, 178-185). In order to define the extent and pattern of subunit relatedness, and to determine the structural basis for possible similarities and differences in subunit functions, we are deducing the primary structures of macropain subunits by cDNA cloning and DNA sequence analysis. We report here the primary structures of four subunits. The data clearly demonstrate that the proteins represent different, but homologous gene products. Surprisingly, no evidence for homology with any other protein, including proteinases, was obtained. These results suggest that macropain is comprised of a previously unidentified family of evolutionarily related polypeptides. Because biochemical data indicate that macropain contains several different proteinase activities, the current results raise the possibility that the macropain complex is composed of a group of novel proteinases, distinct from those of other structurally identifiable proteinase families.

AB - Macropain (proteasome) is a high-molecular-weight proteinase complex composed of at least 13 electrophoretically distinct subunits. Previous work, including peptide mapping and limited amino acid sequencing, suggested that most of the subunits belong to an evolutionarily related group of different gene products (Lee et al. (1990) Biochim. Biophys. Acta. 1037, 178-185). In order to define the extent and pattern of subunit relatedness, and to determine the structural basis for possible similarities and differences in subunit functions, we are deducing the primary structures of macropain subunits by cDNA cloning and DNA sequence analysis. We report here the primary structures of four subunits. The data clearly demonstrate that the proteins represent different, but homologous gene products. Surprisingly, no evidence for homology with any other protein, including proteinases, was obtained. These results suggest that macropain is comprised of a previously unidentified family of evolutionarily related polypeptides. Because biochemical data indicate that macropain contains several different proteinase activities, the current results raise the possibility that the macropain complex is composed of a group of novel proteinases, distinct from those of other structurally identifiable proteinase families.

KW - Macropain

KW - Multicatalytic proteinase

KW - Proteasome

KW - Ubiquitin

UR - http://www.scopus.com/inward/record.url?scp=0025741822&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025741822&partnerID=8YFLogxK

U2 - 10.1016/0167-4838(91)90020-Z

DO - 10.1016/0167-4838(91)90020-Z

M3 - Article

VL - 1079

SP - 29

EP - 38

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 1

ER -