Characterization and expression of two members of the S-adenosylmethionine decarboxylase gene family in carnation flower

Myeong Min Lee, Sun Hi Lee, Ky Young Park

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

S-adenosylmethionine decarboxylase (SAM DC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. In order to provide information on the structure and regulation of SAMDC, we have isolated and sequenced two different SAMDC cDNA clones from carnation petals. The nucleotide sequences of CSDC9 and CSDC16 show 78.3% identity, and the deduced amino acid sequences show 81.7% identity and 86.5% similarity [12]. There are several regions with highly conserved sequences among SAMDC cDNAs of potato, spinach, periwinkle, man and yeast. These conserved regions include a cleavage site for the processing of SAMDC proenzyme and a putative PEST sequence that may be relevant to the rapid degradation of SAMDC protein. Carnation SAMDC cDNAs have long transcript leaders of 472 bp and 502 bp for CSDC9 and CSDC16, respectively. Both sequences contain short upstream open reading frames (uORFs) in their 5'-untranslated regions. The CSDC9 uORF is 54 amino acids from 152 to 317 while the corresponding sequence in CSDC16 is 52 amino acids located from 156 to 314 in each 5'-untranslated region. The nucleotide sequences of uORFs in CSDC9 and CSDC16 were 89.9% identical. In vitro transcription/translation experiments showed: (1) each proenzyme of both cDNAs of SAMDC was converted to two polypeptides consisting of a large subunit (calculated as 31 544 Da and 32 537 Da, respectively) and a small subunit (calculated as 9704 and 9041 Da, respectively) after 20 min of translation; (2) the processing occurs rapidly during the translation of protein. But once the translation process is stopped accumulation of the subunits slows and never roaches completion even after 300 min. The processing of carnation SAMDC enzyme is not stimulated by putrescine in in vitro transcription/translation reaction.

Original languageEnglish
Pages (from-to)371-382
Number of pages12
JournalPlant Molecular Biology
Volume34
Issue number3
DOIs
Publication statusPublished - 1997 Jun 1

Fingerprint

Dianthus
Adenosylmethionine Decarboxylase
adenosylmethionine decarboxylase
Dianthus caryophyllus
translation (genetics)
Complementary DNA
Genes
Open Reading Frames
5' untranslated regions
flowers
Enzyme Precursors
5' Untranslated Regions
Biosynthesis
zymogens
Transcription
open reading frames
Amino Acids
genes
Nucleotides
Processing

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Genetics
  • Plant Science

Cite this

@article{c751fd4b863141f18513f875cba1ee13,
title = "Characterization and expression of two members of the S-adenosylmethionine decarboxylase gene family in carnation flower",
abstract = "S-adenosylmethionine decarboxylase (SAM DC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. In order to provide information on the structure and regulation of SAMDC, we have isolated and sequenced two different SAMDC cDNA clones from carnation petals. The nucleotide sequences of CSDC9 and CSDC16 show 78.3{\%} identity, and the deduced amino acid sequences show 81.7{\%} identity and 86.5{\%} similarity [12]. There are several regions with highly conserved sequences among SAMDC cDNAs of potato, spinach, periwinkle, man and yeast. These conserved regions include a cleavage site for the processing of SAMDC proenzyme and a putative PEST sequence that may be relevant to the rapid degradation of SAMDC protein. Carnation SAMDC cDNAs have long transcript leaders of 472 bp and 502 bp for CSDC9 and CSDC16, respectively. Both sequences contain short upstream open reading frames (uORFs) in their 5'-untranslated regions. The CSDC9 uORF is 54 amino acids from 152 to 317 while the corresponding sequence in CSDC16 is 52 amino acids located from 156 to 314 in each 5'-untranslated region. The nucleotide sequences of uORFs in CSDC9 and CSDC16 were 89.9{\%} identical. In vitro transcription/translation experiments showed: (1) each proenzyme of both cDNAs of SAMDC was converted to two polypeptides consisting of a large subunit (calculated as 31 544 Da and 32 537 Da, respectively) and a small subunit (calculated as 9704 and 9041 Da, respectively) after 20 min of translation; (2) the processing occurs rapidly during the translation of protein. But once the translation process is stopped accumulation of the subunits slows and never roaches completion even after 300 min. The processing of carnation SAMDC enzyme is not stimulated by putrescine in in vitro transcription/translation reaction.",
author = "Lee, {Myeong Min} and Lee, {Sun Hi} and Park, {Ky Young}",
year = "1997",
month = "6",
day = "1",
doi = "10.1023/A:1005811229988",
language = "English",
volume = "34",
pages = "371--382",
journal = "Plant Molecular Biology",
issn = "0167-4412",
publisher = "Springer Netherlands",
number = "3",

}

Characterization and expression of two members of the S-adenosylmethionine decarboxylase gene family in carnation flower. / Lee, Myeong Min; Lee, Sun Hi; Park, Ky Young.

In: Plant Molecular Biology, Vol. 34, No. 3, 01.06.1997, p. 371-382.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterization and expression of two members of the S-adenosylmethionine decarboxylase gene family in carnation flower

AU - Lee, Myeong Min

AU - Lee, Sun Hi

AU - Park, Ky Young

PY - 1997/6/1

Y1 - 1997/6/1

N2 - S-adenosylmethionine decarboxylase (SAM DC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. In order to provide information on the structure and regulation of SAMDC, we have isolated and sequenced two different SAMDC cDNA clones from carnation petals. The nucleotide sequences of CSDC9 and CSDC16 show 78.3% identity, and the deduced amino acid sequences show 81.7% identity and 86.5% similarity [12]. There are several regions with highly conserved sequences among SAMDC cDNAs of potato, spinach, periwinkle, man and yeast. These conserved regions include a cleavage site for the processing of SAMDC proenzyme and a putative PEST sequence that may be relevant to the rapid degradation of SAMDC protein. Carnation SAMDC cDNAs have long transcript leaders of 472 bp and 502 bp for CSDC9 and CSDC16, respectively. Both sequences contain short upstream open reading frames (uORFs) in their 5'-untranslated regions. The CSDC9 uORF is 54 amino acids from 152 to 317 while the corresponding sequence in CSDC16 is 52 amino acids located from 156 to 314 in each 5'-untranslated region. The nucleotide sequences of uORFs in CSDC9 and CSDC16 were 89.9% identical. In vitro transcription/translation experiments showed: (1) each proenzyme of both cDNAs of SAMDC was converted to two polypeptides consisting of a large subunit (calculated as 31 544 Da and 32 537 Da, respectively) and a small subunit (calculated as 9704 and 9041 Da, respectively) after 20 min of translation; (2) the processing occurs rapidly during the translation of protein. But once the translation process is stopped accumulation of the subunits slows and never roaches completion even after 300 min. The processing of carnation SAMDC enzyme is not stimulated by putrescine in in vitro transcription/translation reaction.

AB - S-adenosylmethionine decarboxylase (SAM DC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine. In order to provide information on the structure and regulation of SAMDC, we have isolated and sequenced two different SAMDC cDNA clones from carnation petals. The nucleotide sequences of CSDC9 and CSDC16 show 78.3% identity, and the deduced amino acid sequences show 81.7% identity and 86.5% similarity [12]. There are several regions with highly conserved sequences among SAMDC cDNAs of potato, spinach, periwinkle, man and yeast. These conserved regions include a cleavage site for the processing of SAMDC proenzyme and a putative PEST sequence that may be relevant to the rapid degradation of SAMDC protein. Carnation SAMDC cDNAs have long transcript leaders of 472 bp and 502 bp for CSDC9 and CSDC16, respectively. Both sequences contain short upstream open reading frames (uORFs) in their 5'-untranslated regions. The CSDC9 uORF is 54 amino acids from 152 to 317 while the corresponding sequence in CSDC16 is 52 amino acids located from 156 to 314 in each 5'-untranslated region. The nucleotide sequences of uORFs in CSDC9 and CSDC16 were 89.9% identical. In vitro transcription/translation experiments showed: (1) each proenzyme of both cDNAs of SAMDC was converted to two polypeptides consisting of a large subunit (calculated as 31 544 Da and 32 537 Da, respectively) and a small subunit (calculated as 9704 and 9041 Da, respectively) after 20 min of translation; (2) the processing occurs rapidly during the translation of protein. But once the translation process is stopped accumulation of the subunits slows and never roaches completion even after 300 min. The processing of carnation SAMDC enzyme is not stimulated by putrescine in in vitro transcription/translation reaction.

UR - http://www.scopus.com/inward/record.url?scp=1842377104&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1842377104&partnerID=8YFLogxK

U2 - 10.1023/A:1005811229988

DO - 10.1023/A:1005811229988

M3 - Article

C2 - 9225849

AN - SCOPUS:1842377104

VL - 34

SP - 371

EP - 382

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 3

ER -