Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase

E. Lauze, B. Stoelcker, F. C. Luca, E. Weiss, A. R. Schutz, Mark Winey

Research output: Contribution to journalArticle

117 Citations (Scopus)

Abstract

The MPS1 gene has been previously identified by a mutant allele that shows defects in spindle pole body (SPB) duplication and cell cycle control. The SPB is the centrosome-equivalent organelle in the yeast Saccharomyces cerevisiae, and it nucleates all the microtubules in the cell. We report the isolation of the MPS1 gene, which encodes an essential protein kinase homolog. The MPS1 open reading frame has been fused to those that encode the LexA protein or the GST protein and both of these constructs function in yeast. The fusion proteins have been affinity-purified from yeast extracts and the GST chimeric protein has been found to be a phosphoprotein. Both proteins have been used to demonstrate intrinsic in vitro protein kinase activity of Mps1p against exogenous substrates and itself (autophosphorylation). A mutation predicted to abolish kinase function not only eliminates in vitro protein kinase activity, but also behaves like a null mutation in vivo, suggesting that kinase activity contributes to the essential function of the protein. Phosphoamino acid analysis of substrates phosphorylated by Mps1p indicates that this kinase can phosphorylate serine, threonine and tyrosine residues, identifying Mps1p as a dual specificity protein kinase.

Original languageEnglish (US)
Pages (from-to)1655-1663
Number of pages9
JournalEMBO Journal
Volume14
Issue number8
StatePublished - Jan 1 1995
Externally publishedYes

Fingerprint

Spindle Pole Bodies
Gene Duplication
Yeast
Protein Kinases
Poles
Genes
Yeasts
Proteins
Phosphotransferases
Phosphoamino Acids
Centrosome
Mutation
Phosphoproteins
Substrates
Threonine
Cell Cycle Checkpoints
Microtubules
Organelles
Serine
Open Reading Frames

Keywords

  • Mitosis
  • MPS1
  • Protein kinase
  • Spindle pole body
  • Yeast

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Lauze, E., Stoelcker, B., Luca, F. C., Weiss, E., Schutz, A. R., & Winey, M. (1995). Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase. EMBO Journal, 14(8), 1655-1663.

Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase. / Lauze, E.; Stoelcker, B.; Luca, F. C.; Weiss, E.; Schutz, A. R.; Winey, Mark.

In: EMBO Journal, Vol. 14, No. 8, 01.01.1995, p. 1655-1663.

Research output: Contribution to journalArticle

Lauze, E, Stoelcker, B, Luca, FC, Weiss, E, Schutz, AR & Winey, M 1995, 'Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase', EMBO Journal, vol. 14, no. 8, pp. 1655-1663.
Lauze E, Stoelcker B, Luca FC, Weiss E, Schutz AR, Winey M. Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase. EMBO Journal. 1995 Jan 1;14(8):1655-1663.
Lauze, E. ; Stoelcker, B. ; Luca, F. C. ; Weiss, E. ; Schutz, A. R. ; Winey, Mark. / Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase. In: EMBO Journal. 1995 ; Vol. 14, No. 8. pp. 1655-1663.
@article{3ce152929aea445cbe8b50ef54fff982,
title = "Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase",
abstract = "The MPS1 gene has been previously identified by a mutant allele that shows defects in spindle pole body (SPB) duplication and cell cycle control. The SPB is the centrosome-equivalent organelle in the yeast Saccharomyces cerevisiae, and it nucleates all the microtubules in the cell. We report the isolation of the MPS1 gene, which encodes an essential protein kinase homolog. The MPS1 open reading frame has been fused to those that encode the LexA protein or the GST protein and both of these constructs function in yeast. The fusion proteins have been affinity-purified from yeast extracts and the GST chimeric protein has been found to be a phosphoprotein. Both proteins have been used to demonstrate intrinsic in vitro protein kinase activity of Mps1p against exogenous substrates and itself (autophosphorylation). A mutation predicted to abolish kinase function not only eliminates in vitro protein kinase activity, but also behaves like a null mutation in vivo, suggesting that kinase activity contributes to the essential function of the protein. Phosphoamino acid analysis of substrates phosphorylated by Mps1p indicates that this kinase can phosphorylate serine, threonine and tyrosine residues, identifying Mps1p as a dual specificity protein kinase.",
keywords = "Mitosis, MPS1, Protein kinase, Spindle pole body, Yeast",
author = "E. Lauze and B. Stoelcker and Luca, {F. C.} and E. Weiss and Schutz, {A. R.} and Mark Winey",
year = "1995",
month = "1",
day = "1",
language = "English (US)",
volume = "14",
pages = "1655--1663",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "8",

}

TY - JOUR

T1 - Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase

AU - Lauze, E.

AU - Stoelcker, B.

AU - Luca, F. C.

AU - Weiss, E.

AU - Schutz, A. R.

AU - Winey, Mark

PY - 1995/1/1

Y1 - 1995/1/1

N2 - The MPS1 gene has been previously identified by a mutant allele that shows defects in spindle pole body (SPB) duplication and cell cycle control. The SPB is the centrosome-equivalent organelle in the yeast Saccharomyces cerevisiae, and it nucleates all the microtubules in the cell. We report the isolation of the MPS1 gene, which encodes an essential protein kinase homolog. The MPS1 open reading frame has been fused to those that encode the LexA protein or the GST protein and both of these constructs function in yeast. The fusion proteins have been affinity-purified from yeast extracts and the GST chimeric protein has been found to be a phosphoprotein. Both proteins have been used to demonstrate intrinsic in vitro protein kinase activity of Mps1p against exogenous substrates and itself (autophosphorylation). A mutation predicted to abolish kinase function not only eliminates in vitro protein kinase activity, but also behaves like a null mutation in vivo, suggesting that kinase activity contributes to the essential function of the protein. Phosphoamino acid analysis of substrates phosphorylated by Mps1p indicates that this kinase can phosphorylate serine, threonine and tyrosine residues, identifying Mps1p as a dual specificity protein kinase.

AB - The MPS1 gene has been previously identified by a mutant allele that shows defects in spindle pole body (SPB) duplication and cell cycle control. The SPB is the centrosome-equivalent organelle in the yeast Saccharomyces cerevisiae, and it nucleates all the microtubules in the cell. We report the isolation of the MPS1 gene, which encodes an essential protein kinase homolog. The MPS1 open reading frame has been fused to those that encode the LexA protein or the GST protein and both of these constructs function in yeast. The fusion proteins have been affinity-purified from yeast extracts and the GST chimeric protein has been found to be a phosphoprotein. Both proteins have been used to demonstrate intrinsic in vitro protein kinase activity of Mps1p against exogenous substrates and itself (autophosphorylation). A mutation predicted to abolish kinase function not only eliminates in vitro protein kinase activity, but also behaves like a null mutation in vivo, suggesting that kinase activity contributes to the essential function of the protein. Phosphoamino acid analysis of substrates phosphorylated by Mps1p indicates that this kinase can phosphorylate serine, threonine and tyrosine residues, identifying Mps1p as a dual specificity protein kinase.

KW - Mitosis

KW - MPS1

KW - Protein kinase

KW - Spindle pole body

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=0029008377&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029008377&partnerID=8YFLogxK

M3 - Article

VL - 14

SP - 1655

EP - 1663

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 8

ER -