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J Biol Chem, Vol. 275, Issue 13, 9673-9683, March 31, 2000
From the Myristoyl-CoA:protein
N-myristoyltransferase (NMT, EC 2.3.1.97) catalyzes the
co-translational addition of myristic acid to the amino-terminal
glycine residue of a number of important proteins of diverse functions.
We have isolated a full-length Arabidopsis thaliana
cDNA encoding NMT (AtNMT1), the first described from a
higher plant. This AtNMT1 cDNA clone has an open
reading frame of 434 amino acids and a predicted molecular mass of
48,706 Da. The primary structure is 50% identical to the mammalian
NMTs. Analyses of Southern blots, genomic clones, and database
sequences suggested that the A. thaliana genome contains
two copies of NMT gene, which are present on different
chromosomes and have distinct genomic organizations. The recombinant
AtNMT1 expressed in Escherichia coli exhibited a high
catalytic efficiency for the peptides derived from putative plant
myristoylated proteins AtCDPK6 and Fen kinase. The AtNMT was similar to
the mammalian NMTs with respect to a relative specificity for myristoyl
CoA amoung the acyl CoA donors and also inhibition by the bovine brain
NMT inhibitor NIP71. The AtNMT1 expression
profile indicated ubiquity in roots, stem, leaves, flowers, and
siliques ( The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF193616.
Molecular Cloning, Genomic Organization, and Biochemical
Characterization of Myristoyl-CoA:Protein
N-Myristoyltransferase from Arabidopsis
thaliana*
§,,,
,,**
National Research Council of Canada, Plant
Biotechnology Institute, Saskatoon S7N 0W9 and the ¶ Department
of Pathology and Saskatoon Cancer Center, University of Saskatchewan,
Saskatoon S7N 4H4, Saskatchewan, Canada
1.7 kb transcript and 50 kDa immunoreactive polypeptide) but a greater level in the younger tissue, which are
developmentally very active. NMT activity was also evident in all these
tissues. Subcellular distribution studies indicated that, in leaf
extracts, ~60% of AtNMT activity was associated with the ribosomal
fractions, whereas ~30% of the activity was observed in the
cytosolic fractions. The NMT is biologically important to plants, as
noted from the stunted development when the AtNMT1 was down-regulated
in transgenic Arabidopsis under the control of an enhanced
CaMV 35S promoter. The results presented in this study provide the
first direct molecular evidence for plant protein N-myristoylation and a mechanistic basis for understanding
the role of this protein modification in plants.
*
This is publication number 42625 from the National Research
Council of Canada.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Current address: Agriculture & Agri-Food Canada, Saskatoon
Research Center, Saskatoon S7N 0X2, Saskatchewan, Canada.
**
To whom correspondence should be addressed: National Research
Council of Canada, Plant Biotechnology Institute, 110 Gymnasium Place,
Saskatoon S7N 0W9, Saskatchewan, Canada. Tel.: 306-975-5267; Fax:
306-975-4839; E-mail: raju.datla@pbi.nrc.ca.
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