The mouse has a Polycomb-like chromobox gene

Development ◽  
1992 ◽  
Vol 114 (4) ◽  
pp. 921-929 ◽  
Author(s):  
J.J. Pearce ◽  
P.B. Singh ◽  
S.J. Gaunt
Keyword(s):  
Cellular Proliferation ◽  
Expression Patterns ◽  
Northern Analysis ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Drosophila Gene ◽  
Acid Protein ◽  
Temporal And Spatial ◽  
Amino Acid Protein

The Drosophila gene Polycomb (Pc) has been implicated in the clonal inheritance of determined states and is a trans-regulator of the Antennapedia-like homeobox genes. Pc shares a region of homology (the chromobox) with the Drosophila gene Heterochromatin Protein 1 (HP1), a component of heterochromatin. The Pc chromobox has been used to isolate a mouse chromobox gene, M33, which encodes a predicted 519 amino acid protein. The M33 chromodomain is more similar to that in the Pc protein, than that in the HP1 protein. In addition to the chromodomain, the M33 and Pc proteins also share a region of homology at their C termini. The temporal and spatial expression patterns of M33 have been studied by in situ hybridization and northern analysis. During the final 10 days of embryonic development, M33 expression mirrors that of the cell-cycle-specific cyclin B gene. It is therefore suggested that the rate of cellular proliferation controls M33 expression. From comparisons of the characteristics of M33 with those of Pc it is proposed that M33 is a Pc-like chromobox gene. The roles of M33 and Pc in models of cellular memory are examined and implications of the memory models addressed.

Αλληλεπιδράσεις και in situ οργάνωση διαμεμβρανικών πρωτεϊνών του πυρηνικού φακέλου

2006 ◽  
Author(s):  
Δήμητρα Μακατσώρη
Keyword(s):  
Binding Site ◽  
Heterochromatin Protein 1 ◽  
Heterochromatin Protein ◽  
Histone Fold ◽  
Β Receptor

Αρχικός έλεγχος φυσιολογικών και νεοπλασματικών κυττάρων ανθρώπου και ποντικού χρησιμοποιώντας ειδικούς ανιχνευτές για την HPΙα και ΗΡΙβ έδειξε ότι η έκφραση των πρωτεϊνών αυτών δεν διαφέρει σημαντικά. Παράλληλα, μελέτη φυσιολογικών ιστών και πρωτογενών καλλιεργειών που έγινε στο εργαστήριό μας έδειξε σύνθετα πρότυπα υποπυρηνικής κατανομής που δεν θα μπορούσαν εύκολα να αποδοθούν σε αυξομειώσεις της ενδοκυττάριας συγκέντρωσης των ΗΡΙα/β, αλλά θα ήταν πιο συμβατά με έναν μηχανισμό ρύθμισης που εξαρτάται από αυξητικούς παράγοντες και μιτογόνα. Επί τη βάσει αυτών των δεδομένων επικεντρώσαμε τη μελέτη μας στις αλληλεπιδράσεις της πρωτεΐνης ΗΡ1 (Heterochromatin Protein 1) με διαφορετικά χρωματινικά υποστρώματα υπό in vitro και in vivo συνθήκες. Η άποψη που ισχύει ως τώρα είναι ότι η ΗΡ1 εντοπίζεται σε μεταγραφικά ανενεργή, συστατική (constitutive) ετεροχρωματίνη συνδεόμενη ειδικά με την ιστόνη Η3 που είναι μετα-μεταφραστικά τροποποιημένη (τριμεθυλιωμένη) στη λυσίνη 9 (me3K9-H3). Το παραπάνω πρότυπο, παρά την κομψότητα και την απλότητά του δεν επαρκεί όμως για να ερμηνεύσει το ευρύ φάσμα των αλληλεπιδράσεων της ΗΡ1 με την ετεροχρωματίνη πουπαρατηρούνται in vivo. Για αυτόν τον λόγο, μελετήσαμε τις αλληλεπιδράσεις ΗΡ1- χρωματίνης σε διαφορετικά επίπεδα πολυπλοκότητας και διερευνήσαμε κατά πόσον η me3K9-H3 αποτελεί τη μοναδική θέση πρόσδεσης της ΗΡ1. In vitro μελέτες έδειξαν ότι η ΗΡ1 προσδένεται επιλεκτικά σε μη τροποποιημένη ή μερικώς πρωτεολυμένη ιστόνη Η3, αλληλεπιδρώντας κυρίως με το κεντρικό τμήμα της (histone fold). Επίσης δείξαμε ότι η ΗΡ1 συνδέεται πιο ισχυρά στα διασπασμένα νουκλεοσώματα (Η3/Η4 υποσωματίδια) από ότι στα ακέραια σωματίδια. Τα αποτελέσματα της ανοσοαποτύπωσης κατά western και της φασματοσκοπίας μάζας έδειξαν ότι τα σωματίδια που επιλέγει η ΗΡ1 διαθέτουν ένα πολύπλοκο μοτίβο μετα-μεταφραστικών τροποποιήσεων, δεν είναι ιδιαίτερα εμπλουτισμένασε me3K9-H3 και δεν ακολουθούν το σύνολο των κανόνων που υπαγορεύονται από τον ιστονικό κώδικα. Αυτές οι βιοχημικές μελέτες συνηγορούν στην ιδέα ότι οι πρωτεΐνες ΗΡ1 αλληλεπιδρούν μετα διαφορετικά χρωματινικά υποστρώματα με τρόπο που εξαρτάται από τη φυσική κατάσταση της χρωματίνης. Είναι επίσης φανερό ότι οι in vitro παρατηρήσεις μας σχετίζονται με μία τουλάχιστον «χρωματινική κατάσταση» που απαντάται in vivo. Για παράδειγμα, παρατηρήσαμε ότι, η HP1 και η me3K9-H3 δεν συνεντοπίζονται απόλυτα και παρουσιάζουν διακριτά πρότυπα. In vivo πειράματα έδειξαν επίσης ότι η σταθερή ενσωμάτωση της ΗΡ1 στις ετεροχρωματινικές εστίες εξαρτάται από την S φάση. Τα αποτελέσματα αυτά αμφισβητούν το δόγμα ότι η μεθυλίωση στη λυσίνη 9 της ιστόνης Η3 αποτελεί τη μοναδική θέση πρόσδεσης (creates a binding site...) για την ΗΡ1 καιυποστηρίζουν ένα μηχανισμό ενσωμάτωσης που βασίζεται στην αντιγραφή. Ένα άλλο τμήμα της μελέτης μας επικεντρώθηκε στις αλληλεπιδράσεις του πυρηνικού φακέλου με την ετεροχρωματίνη. Ένα βασικό συστατικό του πυρηνικού φακέλου είναι ο LBR (Lamin Β Receptor), μία πολυτοπική πρωτεΐνη της εσωτερικής πυρηνικής μεμβράνης που συμμετέχει στην αγκυροβόληση της χρωματίνης στην περιφέρεια. Δύο βασικοί παράμετροι στις αλληλεπιδράσεις LBR-χρωματίνης είναι η φυσική κατάσταση του LBR και τα μοριακά χαρακτηριστικά της χρωματίνης με την οποία συνδέεται. Για να προσεγγίσουμε τα ερωτήματα αυτά, απομονώσαμε τμήματα περιφερικής ετεροχρωματίνης που είναι προσκολλημένα στην εσωτερική πυρηνική μεμβράνη. Δείξαμε ότι το αμινοτελικό τμήμα του LBR συνδέεται άμεσα με μονονουκλεοσώματα. Ανάλυση των νουκλεοσωματικών σωματιδίων που αλληλεπιδρούν με τον LBR με φασματοσκοπία μάζας απεκάλυψε πολύπλοκα πρότυπα μεθυλιωμένων/ακετυλιωμένων ιστονών που δεν περιέχουν ευχρωματινικές επιγενετικές τροποποιήσεις. Επίσης, μερικοί από τους συνδυασμούς που ανιχνεύθηκαν δεν ήταν συμβατοί με τους κανόνες του «ιστονικού κώδικα». Πολλές από τις διαμεμβρανικές πρωτεΐνες του πυρηνικού φακέλου οργανώνονται σε πολυπρωτεϊνικά σύμπλοκα και σχηματίζουν πλατφόρμες αναδιαμόρφωσης χρωματίνης. Πειράματα in vitro έδειξαν ότι ο LBR αλληλεπιδρά με τον εαυτό του μέσω του αμινοτελικού τμήματος και σχηματίζει ολιγομερή στο επίπεδο του πυρηνικού φακέλου. Επίσης, χρησιμοποιώντας μία ποικιλία μορφολογικών τεχνικών, δείξαμε ότι ο ενδογενής LBRεντοπίζεται σε διακριτές νησίδες στον πυρηνικό φάκελο. Τέλος, μορφολογική ανάλυση τωνετερόζυγων μεταλλάξεων του LBR στα ποντίκια έδειξε ότι η φυσιολογική κατανομή καθώς και η οργάνωση των νησίδων που σχηματίζει ο LBR στον φάκελο διαταράσσεται σημαντικά προκαλώντας μία ποικιλία δομικών και πυρηνικών αλλοιώσεων

scholarly journals Identification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein

1993 ◽  
Vol 105 (3) ◽  
pp. 777-785 ◽  
Author(s):  
A.B. Vojtek ◽  
J.A. Cooper
Keyword(s):  
Adenylyl Cyclase ◽  
Leading Edge ◽  
Northern Analysis ◽  
Reading Frame ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Acid Protein ◽  
Carboxy Terminal ◽  
Amino Acid Protein

CAP, an adenylyl cyclase associated protein, is present in Saccharomyces cerevisiae and Schizosaccharomyces pombe. In both organisms, CAP is bifunctional: the N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to respond appropriately to upstream regulatory signals, such as RAS in S. cerevisiae; the C-terminal domain is required for cellular morphogenesis. Here, we describe the isolation of a cDNA encoding a CAP homolog from a higher eukaryote. The mouse CAP cDNA contains an open reading frame capable of encoding a 474 amino acid protein. The protein encoded by the mouse CAP cDNA shows extensive homology to the yeast CAP proteins, particularly in the central poly-proline rich region and in the C-terminal domain. By northern analysis, the CAP message appears to be ubiquitous, but not uniform. By indirect immunofluorescence, ectopically expressed mouse CAP protein is found in the cytoplasm of fibroblasts and, in migrating cells, at the leading edge. Expression of the mouse CAP cDNA in S. cerevisiae complements defects associated with loss of the yeast CAP carboxy-terminal domain. Hence, the function of the CAP carboxy-terminal domain has been conserved from yeast to mouse.

Expression of Erythropoietin Receptor-Like Molecule in Xenopus laevis (xeEPOR) and the Development of Anemia by the Administration of Its Recombinant Soluble Form.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 2783-2783
Author(s):  
Youichi Aizawa ◽  
Nami Nogawa ◽  
Nobuyoshi Kosaka ◽  
Yasutaka Maeda ◽  
Takafumi Watanabe ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Peripheral Blood ◽  
Cellular Proliferation ◽  
Physiological Role ◽  
Soluble Form ◽  
Northern Analysis ◽  
Binding Motif ◽  
Normal Peripheral Blood ◽  
Peripheral Erythrocyte

Abstract The regulation of hematopoiesis in non-mammalian vertebrates is poorly understood. This is partly because the structures and effects of most hematopoietic regulators have not been identified. As a first step towards studies on the key ingredient of hematopoietic regulation among phyla as well as the diversity of organisms, we have focused on amphibian hematopoiesis. In this study, a cDNA sharing the highest degree of homology with mammalian erythropoietin (EPO) receptors, named xeEPOR tentatively, was cloned from cDNA library of Xenopus immature erythrocytes. The identities of the deduced entire amino acid sequence to human and murine EPO receptors were 24% and 25%, respectively; whereas transmembrane region and motifs of WSXWS and Box1/2 domains were found in the molecule. The northern analysis revealed that two types of xeEPOR RNAs were expressed in normal peripheral blood cells. In addition, by in situ hybridization and immunostaining with monoclonal antibodies raised against the extracellular domain of xeEPOR (soluble xeEPOR), immature basophilic erythrocytes expressing xeEPOR appeared in peripheral blood of phenylhydrazine-treated adult Xenopus. The fulllength xeEPOR cDNA was introduced into murine FDC/P2 cells and the signaling for the cellular proliferation and differentiation was examined in the presence of serum derived from anemic Xenopus as a stimulator. To further understanding the contribution of the xeEPOR gene expression to primitive and definitive hematopoiesis on Xenopus development, whole mount in situ hybridization was performed. As the binding motif of GATA-1, the hematopoietic specific transcription factor, was located at −24 to −15 base upstream of the translation initiation sequence, the correlated expressions of xeEPOR and Xenopus GATA-1 on developing embryo were evaluated with RT-PCR. The xeEPOR RNA was abundantly expressed at Nieuwkoop stage 30 (blood island formation) and thereafter, and temporally followed the expression of GATA-1, suggesting that the functional expression of xeEPOR was upregulated by GATA-1 in Xenopus as reported in studies on mammalian erythropoiesis. To confirm biological functions of the molecule, soluble xeEPOR was administered into adult Xenopus by intracardiac consecutive injections. The peripheral erythrocyte counts were gradually decreased; meanwhile immature erythrocytes were emerged in the circulation, demonstrating that this molecule plays a significant physiological role in erythropoiesis in Xenopus.

scholarly journals NOP3 is an essential yeast protein which is required for pre-rRNA processing.

1992 ◽  
Vol 119 (4) ◽  
pp. 737-747 ◽  
Author(s):  
I D Russell ◽  
D Tollervey
Keyword(s):  
Northern Analysis ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Rrna Processing ◽  
Reading Frame ◽  
Repeat Units ◽  
Nucleolar Proteins ◽  
Acid Protein ◽  
Sds Page ◽  
Amino Acid Protein

The four nucleolar proteins NOP1, SSB1, GAR1, and NSR1 of Saccharomyces cerevisiae share a repetitive domain composed of repeat units rich in glycine and arginine (GAR domain). We have cloned and sequenced a fifth member of this family, NOP3, and shown it to be essential for cell viability. The NOP3 open reading frame encodes a 415 amino acid protein with a predicted molecular mass of 45 kD, containing a GAR domain and an RNA recognition motif. NOP3-specific antibodies recognize a 60-kD protein by SDS-PAGE and decorate the nucleolus and the surrounding nucleoplasm. A conditional lethal mutation, GAL::nop3, was constructed; growth of the mutant strain in glucose medium represses NOP3 expression. In cells depleted of NOP3, production of cytoplasmic ribosomes is impaired. Northern analysis and pulse-chase labeling indicate that pre-rRNA processing is inhibited at the late steps, in which 27SB pre-rRNA is cleaved to 25S rRNA and 20S pre-rRNA to 18S rRNA.

Analysis of an enhancer trap expressed in regenerating Drosophila imaginal discs

Genome ◽  
1995 ◽  
Vol 38 (4) ◽  
pp. 724-736 ◽  
Author(s):  
William R. Addison ◽  
William J. Brook ◽  
Laura D. Querengesser ◽  
Stanley Y. K. Tiong ◽  
Michael A. Russell
Keyword(s):  
Expression Patterns ◽  
Imaginal Discs ◽  
Enhancer Trap ◽  
Northern Analysis ◽  
Neural Cells ◽  
Cell Fates ◽  
Imprecise Excision ◽  
Selector Genes ◽  
Sensory Neural

In Drosophila, imaginal discs are the undifferentiated larval precursors of the pattern of epidermal and sensory neural cells in each adult segment. Although cell fates are already specified by late third instar, disc fragments can either regenerate or duplicate after growth in culture. The outcome depends on signaling between cells across the healed wound and involves a redeployment of the expression patterns of selector genes and other disc pattern genes. We recently used the enhancer-trap method to screen for such genes that are expressed ectopically at the wound-heal site in imaginal discs undergoing regeneration. Here we report the cloning by plasmid rescue of transcribed sequences adjacent to one such enhancer-trap insertion. Using Northern analysis and in situ hybridization we show that one transcript is expressed in the embryo and in imaginal discs in a pattern similar to that of the enhancer trap. We also, by imprecise excision of the enhancer-trap insertion, generated a series of flanking deletions that were mapped using Southern analysis and complementation.Key words: Drosophila, imaginal discs, enhancer traps, regeneration genes.

scholarly journals The role of bone morphogenetic proteins 2, 4, 6 and 7 during ovarian follicular development in sheep: contrast to rat

Reproduction ◽  
2006 ◽  
Vol 131 (3) ◽  
pp. 501-513 ◽  
Author(s):  
Jennifer L Juengel ◽  
Karen L Reader ◽  
Adrian H Bibby ◽  
Stan Lun ◽  
Ian Ross ◽  
...  
Keyword(s):  
Growth Factors ◽  
Granulosa Cell ◽  
Granulosa Cells ◽  
Cellular Proliferation ◽  
Expression Patterns ◽  
Follicular Development ◽  
Cell Functions ◽  
Progesterone Production ◽  
Ovarian Follicular Development

The intraovarian roles of BMP family members such as BMP2, 4, 6 and 7 are not well understood, particularly in species with low ovulation rates such as sheep. Therefore, the objectives of these experiments were to determine the expression patterns of mRNAs encoding BMP2, 4, 6 and 7 during ovarian follicular development in sheep, and to determine the effects of these growth factors on ovine granulosa cell functions in vitro. For comparative purposes, the effects of these BMPs were also determined in rat granulosa cells since these factors have been most widely studied in this poly-ovulatory species. As assessed by in situ hybridization, non-atretic ovine follicles expressed mRNA for BMP6 but not 2, 4 or 7. Furthermore, expression of BMP6 was limited to the oocyte of primordial as well as primary, pre-antral and antral follicles. Reverse transcription-PCR of granulosa cell mRNA detected low levels of all the BMPs in some pools of cells. BMP2, 4, 6 and 7 each inhibited progesterone production from ovine granulosa cells without affecting cellular proliferation/survival. Similarly, these BMPs inhibited progesterone production from rat granulosa cells. However, they also stimulated cellular proliferation/survival of the rat granulosa cells highlighting a species-specific difference for these growth factors. In conclusion, in sheep, BMP2, 4, 6 and 7 inhibit granulosa cell differentiation without affecting proliferation. However, as BMP2, 4 and 7 were not detectable by in situ hybridization in any cells of non-atretic ovarian follicles, it seems unlikely that these proteins would have an important intra-ovarian role in regulating follicular development in sheep. In contrast, localization of BMP6 mRNA in the oocyte suggests that this BMP family member may have a paracrine and/or autocrine role in regulating follicular growth in sheep, as has been shown for two other oocyte derived from members of the transforming growth factor superfamily, BMP15 and growth differentiation factor 9.

scholarly journals Molecular Cloning of NHE3 from LLC-PK1 Cells and Localization in Pig Kidney

1999 ◽  
Vol 10 (8) ◽  
pp. 1649-1657
Author(s):  
CHRISTINE A. SHUGRUE ◽  
NICHOLAS OBERMÜLLER ◽  
SEBASTIAN BACHMANN ◽  
CAROLYN W. SLAYMAN ◽  
ROBERT F. REILLY
Keyword(s):  
Species Differences ◽  
Genomic Library ◽  
Expression Patterns ◽  
Northern Analysis ◽  
Kidney Cortex ◽  
Coding Region ◽  
Pig Kidney ◽  
Reverse Transcription Pcr ◽  
Established Line

Abstract. LLC-PK1 cells, an established line from pig kidney, express basolateral and apical Na+/H+ exchangers that can be distinguished by their differing sensitivities to the amiloride analog N-ethyl-N-isopropylamiloride (EIPA). It has been shown previously that the basolateral exchanger is encoded by NHE1. In the present study, a combination of reverse transcription-PCR, 5′ RACE, and genomic library screening was used to clone the coding region of the porcine NHE3 gene. There was significant homology between the LLC-PK1 sequence and the previously reported rabbit and rat NHE3 genes, with nucleotide and deduced amino acid identities of 87 and 85% in rabbit, and 85 and 87% in rat, respectively. To study expression patterns, Northern analysis was carried out using an NHE3 cDNA to probe poly(A)+ RNA isolated from LLC-PK1 cells, and from pig kidney cortex. In all three cases, a major transcript of 6.1 kb was detected along with two minor transcripts of 4.7 and 3.8 kb. In situ hybridization with two different NHE3 probes gave intense labeling of the distal convoluted tubule in pig kidney but (unexpectedly) no detectable labeling of the proximal tubule. These studies suggest that there are marked species differences in NHE3 expression in the distal nephron.

scholarly journals Expression and activity of L-Myc in normal mouse development.

1996 ◽  
Vol 16 (4) ◽  
pp. 1794-1804 ◽  
Author(s):  
K S Hatton ◽  
K Mahon ◽  
L Chin ◽  
F C Chiu ◽  
H W Lee ◽  
...  
Keyword(s):  
Cellular Proliferation ◽  
System Development ◽  
Expression Patterns ◽  
Nervous System Development ◽  
Mouse Tissue ◽  
Morphological Development ◽  
Mammalian Development ◽  
Mouse Development ◽  
Neuronal Marker

To determine the role of L-Myc in normal mammalian development and its functional relationship to other members of the Myc family, we determined the normal patterns of L-myc gene expression in the developing mouse by RNA in situ hybridization and assessed the phenotypic impact of L-Myc deficiency produced through standard gene targeting methodology. L-myc transcripts were detected in the developing kidney and lung as well as in both the proliferative and the differentiative zones of the brain and neural tube. Despite significant expression of L-myc in developing mouse tissue, homozygous null L-myc mice were found to be viable, reproductively competent, and represented in expected frequencies from heterozygous matings. A detailed histological survey of embryonic and adult tissues, characterization of an embryonic neuronal marker, and measurement of cellular proliferation in situ did not reveal any congenital abnormalities. The lack of an apparent phenotype associated with L-Myc deficiency indicates that L-Myc is dispensable for gross morphological development and argues against a unique role for L-Myc in early central nervous system development as had been previously suggested. Although overlapping expression patterns among myc family members raise the possibility of complementation of L-Myc deficiency by other Myc oncoproteins, compensatory changes in the levels of c- and/or N-myc transcripts were not detected in homozygous null L-myc mice.

Effect of pregnancy and progesterone concentration on expression of genes encoding for transporters or secreted proteins in the bovine endometrium

2010 ◽  
Vol 41 (1) ◽  
pp. 53-62 ◽  
Author(s):  
N. Forde ◽  
T. E. Spencer ◽  
F. W. Bazer ◽  
G. Song ◽  
J. F. Roche ◽  
...  
Keyword(s):  
Expression Patterns ◽  
Transcript Abundance ◽  
Secreted Proteins ◽  
Quantitative Real Time Pcr ◽  
Temporal Expression ◽  
Expression Of Genes ◽  
Genes Encoding ◽  
Temporal And Spatial ◽  
Temporal Expression Pattern

The objective of this study was to determine the temporal and spatial expression patterns of genes encoding transporters, as well as selected secreted proteins that may be regulated by progesterone (P4) and/or the presence of the conceptus in the bovine endometrium. Estrus-synchronized beef heifers were randomly assigned to either: 1) pregnant, high P4; 2) pregnant, normal P4; 3) cyclic, high P4; or 4) cyclic, normal P4. Uteri were collected on days 5, 7, 13, and 16 of the estrous cycle or pregnancy. Localization of mRNAs for ANPEP, CTGF, LPL, LTF, and SLC5A1 in the uteri was determined by radioactive in situ hybridization, and expression quantified in the endometria by quantitative real-time PCR. ANPEP localized to luminal (LE) and superficial glandular (sGE) epithelia of all heifers on days 5 and 7 only. SLC5A1 mRNA was detected in the LE and sGE on days 13 and 16 in all heifers, and expression increased on day 16 in pregnant groups. CTGF localized weakly to the LE and GE on days 5 and 7 but increased on days 13 and 16 with an increase ( P < 0.05) in CTGF expression in high P4 ( day 7) and pregnant heifers ( day 16). Both LPL and LTF localized to the GE only on days 5 and 7. In conclusion we have characterized the temporal expression pattern of these genes and modulation of their transcript abundance by P4 ( CTGF, LPL) and/or the conceptus ( CTGF, SLC5A1) likely modifies the uterine microenvironment, enhancing histotroph composition and contributing to advanced conceptus elongation.

Expression of a Drosophila mRNA is under circadian clock control during pupation

Development ◽  
1989 ◽  
Vol 107 (4) ◽  
pp. 869-880 ◽  
Author(s):  
L.J. Lorenz ◽  
J.C. Hall ◽  
M. Rosbash
Keyword(s):  
Circadian Clock ◽  
Signal Sequence ◽  
Rapid Decay ◽  
Cdna Sequences ◽  
Stage Of Development ◽  
Acid Protein ◽  
Conceptual Translation ◽  
Per Gene ◽  
Amino Acid Protein

Rhythmic eclosion of Drosophila adults requires per gene function. We have found that a previously identified 0.9 kb RNA transcribed from DNA adjacent to per becomes abundantly expressed during pupation, just prior to eclosion. The daily synchronized emergence of young adults, coupled with a subsequent rapid decay of the transcript, is responsible for what previously appeared to be cycling of the 0.9 kb RNA in adults. In situ hybridization analyses localize the 0.9 kb transcript to the epidermis of newly eclosed adults. Conceptual translation of genomic DNA and cDNA sequences predicts that the 0.9 kb transcript produces a 261 amino acid protein containing a putative signal sequence for membrane transport at its amino terminus. Pupae that reach the same stage of development at slightly different times of day show a subsequent synchronized rise in 0.9 kb RNA levels, indicating that the expression of this transcript is under circadian clock control.

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