ELSEVIER Biochimica et Biophysica Acta 1306 (1996) 133-136
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etBiophysica P~ta
Short sequence-paper
Genomic structure of carp mitogen-activated protein kinase kinase 1
gene
Jiann-Horng Leu a, Ming-Shyue Lee b, Kuan-Tien Chen c, Geen-Dong Chang b,
Chen-Kung Chou d, Chang-Jen Huang a,*
a Institute of Biological Chemistry., Academia Sinica, Taipei, Taiwan
b Graduate Institute of Biochemical Sciences, and National Taiwan Uniuersi~, Taipei, Taiwan
c Department of Surgery, Universi~.' Hospital, National Taiwan University, Taipei, Taiwan
o Department of Medical Research, Veterans General Hospital, Taipei, Taiwan
Received 30 November 1995; accepted 16 January 1996
Abstract
Carp mitogen-activated protein kinase kinase 1 (cMKKI) gene was isolated from a liver genomic library. The sequence around the
exon-intron boundaries and 2 kb of the promoter region were determined. Our data indicate that this gene is composed of 11 exons and 10
introns spanning about 9 kb. Multiple potential transcription initiation sites were located by primer extension analysis. Examination of 2
kb of 5'-flanking sequence revealed potential binding sites for a variety of transcription factors such as E2F, Ets-1, GATA-1, Myb,
NF-IL6, Spl, and NF-kB.
Keywords: Genomic DNA sequence; Mitogen-activated protein kinase kinase; (Cyprinus carpio)
Mitogen-activated protein (MAP) kinases, also known
as extracellular signal-regulated kinases (ERKs), are a
family of serine/threonme kinases that mediate intra-
cellular protein phosphorylation events. They have been
shown to participate in a variety of signal transduction
pathways and are rapidly activated in response to various
extracellular stimuli [1-4]. Several subgroups of MAP
kinase have been identified in vertebrates including the
ERK1 and ERK2 [5,6], c-jun amino-terminal kinase (JNK)
[7,8], p38 [9-11], and ERK5 [12].
The activation of MAP kinase is triggered by an up-
stream activator, called MAP kinase kinase (MKK) or
MAPK/ERK kinase (MEK) [13]. MEK is a dual speci-
ficity kinase that phosphorylates MAP kinase on both
tyrosine and threonine re:ddues [14,15], whereas it is acti-
vated and phosphorylated by a further upstream activator
on its serine/threonine residues [16]. Recently, there are
also a growing number of MEKs [12,17,18]. Specific
MEKs have been shown to phosphorylate specific MAP
kinases in a given pathway. For example, MEK1 and
MEK2 phosphorylate ERK1 and ERK2 in the cellular
* Corresponding author. Fax: + 886 2 3635038.
0167-4781/96/$15.00 © 1996 Elsevier Science B.V. All rights reserved
PII S0167-478 1(96)00023- 1
processes such as proliferation, differentiation, and devel-
opment [4,13]. MEK3 and p38 are involved in the cytokine
response [18,19], whereas MEK4 and JNK are shown to
participate in the stress response [18]. More recently, MEK5
and ERK5 have been identified to constitute a new signal
transduction pathway [12].
As an initial step to study signal transduction in fish, we
have cloned a full-length cDNA encoding the carp MAP
kinase kinase 1 (cMKKI) [20]. In this study, we further
determined the genomic structure and the promoter region
of this gene.
A commercially available carp liver lambda FIX II
genomic library (Stratagene, La Jolla, CA, USA) was
screened using the carp cDNA coding for MKK1 [20] as a
probe. The probe was labeled using a DIG DNA Labeling
Kit (Boehringer Mannheim, Mannheim, Germany). Two
genomic clones (M1 and M2) were isolated from the
library. As shown in Fig. 1, the carp MKK1 gene spanned
about 9 kb and was composed of 11 exons and 10 introns.
The sequence around the exon-intron boundaries was de-
termined and shown in Table 1. All exon/intron bound-
aries identified conformed to the GT/AG splice
donor/acceptor rule [23]. Some exons were relatively
small (46 bp to 78 bp), whereas the first and the last exons