Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing

Yoshikazu Ohya, Mark Goebl, Laurie E. Goodman, Sara Petersen-Bjørn, James D. Friesen, Fuyuhiko Tamanoi, Yasuhiro Anraku

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

A 2.3-kilobase pair DNA fragment of the yeast CAL1 gene was cloned by complementation of the cal1-1 mutation, which causes a defect in nuclear division and bud formation (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1984) Mol. & Gen. Genet. 193, 389-394). Nucleotide sequencing of this fragment revealed a single open reading frame (ORF) encoding a polypeptide of 376 amino acids. Comparative analysis of the predicted amino acid sequence has shown that the CAL1 product has similarity to two yeast proteins: the DPR1 (RAM) gene product that is involved in processing of ras protein at the farnesylation step, and the essential ORF2 protein whose structural gene has a head-to-head arrangement with PRP4, which is involved in mRNA processing. Functional homology between CAL1 and DPR1 has also been suggested from genetic evidence that multiple copies of the CAL1 gene suppress the growth defects of a dpr1 null mutant at high temperature. This suppression is Ca2+-dependent, since it was not observed in complete medium containing 200 μM CaCl2 but was apparent in medium containing 100 mM CaCl2. From sequence analysis of the call-1 mutation, together with the alignment of the three gene products, we have concluded that the conserved Gly328 in the C terminus is important for activity. We suggest that the CAL1 protein participates in a ras-like C-terminal modification of proteins involved in nuclear division and bud growth.

Original languageEnglish
Pages (from-to)12356-12360
Number of pages5
JournalJournal of Biological Chemistry
Volume266
Issue number19
StatePublished - 1991
Externally publishedYes

Fingerprint

Random access storage
Yeast
Genes
Yeasts
Cell Nucleus Division
Processing
Protein Prenylation
Viverridae
Amino Acids
ras Proteins
Defects
Mutation
Proteins
Fungal Proteins
Protein Sequence Analysis
Growth
Open Reading Frames
Sequence Analysis
Nucleotides
Messenger RNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ohya, Y., Goebl, M., Goodman, L. E., Petersen-Bjørn, S., Friesen, J. D., Tamanoi, F., & Anraku, Y. (1991). Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing. Journal of Biological Chemistry, 266(19), 12356-12360.

Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing. / Ohya, Yoshikazu; Goebl, Mark; Goodman, Laurie E.; Petersen-Bjørn, Sara; Friesen, James D.; Tamanoi, Fuyuhiko; Anraku, Yasuhiro.

In: Journal of Biological Chemistry, Vol. 266, No. 19, 1991, p. 12356-12360.

Research output: Contribution to journalArticle

Ohya, Y, Goebl, M, Goodman, LE, Petersen-Bjørn, S, Friesen, JD, Tamanoi, F & Anraku, Y 1991, 'Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing', Journal of Biological Chemistry, vol. 266, no. 19, pp. 12356-12360.
Ohya Y, Goebl M, Goodman LE, Petersen-Bjørn S, Friesen JD, Tamanoi F et al. Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing. Journal of Biological Chemistry. 1991;266(19):12356-12360.
Ohya, Yoshikazu ; Goebl, Mark ; Goodman, Laurie E. ; Petersen-Bjørn, Sara ; Friesen, James D. ; Tamanoi, Fuyuhiko ; Anraku, Yasuhiro. / Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 19. pp. 12356-12360.
@article{3e754b86712a413ea71cbd3e5d5ddac8,
title = "Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing",
abstract = "A 2.3-kilobase pair DNA fragment of the yeast CAL1 gene was cloned by complementation of the cal1-1 mutation, which causes a defect in nuclear division and bud formation (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1984) Mol. & Gen. Genet. 193, 389-394). Nucleotide sequencing of this fragment revealed a single open reading frame (ORF) encoding a polypeptide of 376 amino acids. Comparative analysis of the predicted amino acid sequence has shown that the CAL1 product has similarity to two yeast proteins: the DPR1 (RAM) gene product that is involved in processing of ras protein at the farnesylation step, and the essential ORF2 protein whose structural gene has a head-to-head arrangement with PRP4, which is involved in mRNA processing. Functional homology between CAL1 and DPR1 has also been suggested from genetic evidence that multiple copies of the CAL1 gene suppress the growth defects of a dpr1 null mutant at high temperature. This suppression is Ca2+-dependent, since it was not observed in complete medium containing 200 μM CaCl2 but was apparent in medium containing 100 mM CaCl2. From sequence analysis of the call-1 mutation, together with the alignment of the three gene products, we have concluded that the conserved Gly328 in the C terminus is important for activity. We suggest that the CAL1 protein participates in a ras-like C-terminal modification of proteins involved in nuclear division and bud growth.",
author = "Yoshikazu Ohya and Mark Goebl and Goodman, {Laurie E.} and Sara Petersen-Bj{\o}rn and Friesen, {James D.} and Fuyuhiko Tamanoi and Yasuhiro Anraku",
year = "1991",
language = "English",
volume = "266",
pages = "12356--12360",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

TY - JOUR

T1 - Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing

AU - Ohya, Yoshikazu

AU - Goebl, Mark

AU - Goodman, Laurie E.

AU - Petersen-Bjørn, Sara

AU - Friesen, James D.

AU - Tamanoi, Fuyuhiko

AU - Anraku, Yasuhiro

PY - 1991

Y1 - 1991

N2 - A 2.3-kilobase pair DNA fragment of the yeast CAL1 gene was cloned by complementation of the cal1-1 mutation, which causes a defect in nuclear division and bud formation (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1984) Mol. & Gen. Genet. 193, 389-394). Nucleotide sequencing of this fragment revealed a single open reading frame (ORF) encoding a polypeptide of 376 amino acids. Comparative analysis of the predicted amino acid sequence has shown that the CAL1 product has similarity to two yeast proteins: the DPR1 (RAM) gene product that is involved in processing of ras protein at the farnesylation step, and the essential ORF2 protein whose structural gene has a head-to-head arrangement with PRP4, which is involved in mRNA processing. Functional homology between CAL1 and DPR1 has also been suggested from genetic evidence that multiple copies of the CAL1 gene suppress the growth defects of a dpr1 null mutant at high temperature. This suppression is Ca2+-dependent, since it was not observed in complete medium containing 200 μM CaCl2 but was apparent in medium containing 100 mM CaCl2. From sequence analysis of the call-1 mutation, together with the alignment of the three gene products, we have concluded that the conserved Gly328 in the C terminus is important for activity. We suggest that the CAL1 protein participates in a ras-like C-terminal modification of proteins involved in nuclear division and bud growth.

AB - A 2.3-kilobase pair DNA fragment of the yeast CAL1 gene was cloned by complementation of the cal1-1 mutation, which causes a defect in nuclear division and bud formation (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1984) Mol. & Gen. Genet. 193, 389-394). Nucleotide sequencing of this fragment revealed a single open reading frame (ORF) encoding a polypeptide of 376 amino acids. Comparative analysis of the predicted amino acid sequence has shown that the CAL1 product has similarity to two yeast proteins: the DPR1 (RAM) gene product that is involved in processing of ras protein at the farnesylation step, and the essential ORF2 protein whose structural gene has a head-to-head arrangement with PRP4, which is involved in mRNA processing. Functional homology between CAL1 and DPR1 has also been suggested from genetic evidence that multiple copies of the CAL1 gene suppress the growth defects of a dpr1 null mutant at high temperature. This suppression is Ca2+-dependent, since it was not observed in complete medium containing 200 μM CaCl2 but was apparent in medium containing 100 mM CaCl2. From sequence analysis of the call-1 mutation, together with the alignment of the three gene products, we have concluded that the conserved Gly328 in the C terminus is important for activity. We suggest that the CAL1 protein participates in a ras-like C-terminal modification of proteins involved in nuclear division and bud growth.

UR - http://www.scopus.com/inward/record.url?scp=0025823167&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025823167&partnerID=8YFLogxK

M3 - Article

C2 - 2061313

AN - SCOPUS:0025823167

VL - 266

SP - 12356

EP - 12360

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -