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J. Biol. Chem., Vol. 275, Issue 51, 40576-40587, December 22, 2000
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From the Institut de Pharmacologie Moléculaire et
Cellulaire-CNRS UPR 411, 660 Route des Lucioles-Sophia-Antipolis,
06560 Valbonne, France
Melanin-concentrating hormone (MCH) mRNA
expression is induced by nerve growth factor and lithium in PC12 cells,
whereas three large MCH RNA species are found in untreated cells. In
this study, we investigated the structures, regulations of expression,
and putative functions of these transcripts. Northern blot, rapid amplification of cDNA ends-polymerase chain reaction, reverse transcriptase-polymerase chain reaction, and sequencing experiments demonstrated that they are antisense RNAs complementary to the MCH gene. Two classes of antisense RNAs could be
discriminated as follows: 1) non-coding unspliced RNAs that overlap
mainly the coding part of the MCH gene; 2) spliced variant
mRNAs complementary to the 3'-flanking end of the MCH
gene and that encode putative proteins containing DNA/RNA binding
domains. We named this new transcriptional unit AROM for
antisense-RNA-overlapping-MCH
gene. Spliced variant AROM mRNAs are expressed in a broad range of
rat organs. Western blot and immunohistochemistry experiments revealed several proteins with cytoplasmic but also nuclear localization in PC12
cells. Time course studies during nerve growth factor and lithium
treatment of PC12 cells indicated a reciprocal regulation of the
MCH and AROM gene transcripts, reflected also
at the level of AROM proteins. The major translational product is a
64-kDa protein (AROM-p64). Recombinant AROM-p64 displayed high binding to single-stranded DNA and poly(A) homopolymers suggesting that this
protein could play a role in mRNA maturation/metabolism.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF303035.
The AROM Gene, Spliced mRNAs Encoding New
DNA/RNA-binding Proteins Are Transcribed from the Opposite Strand of
the Melanin-concentrating Hormone Gene in Mammals*
,
*
This work was supported in part by the MENRT Grant 95G0099,
the "Association Française Contre les Myopathies" (AFM) Grant ASI 1996-1998, and by the CNRS.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.
Recipient of a "Ministère de l'Education Nationale"
Fellowship Allocation 1996-1999 and is presently supported by the
"Association pour la Recherche Contre le Cancer" (ARC 2000).
§
To whom correspondence should be addressed. Tel.: 33 493 95 77 53;
Fax: 33 493 95 77 08; E-mail: nahonjl@ipmc.cnrs.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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