Molecular cloning, characterization, and expression analysis of a QM homologue in the ant Polyrhachis vicina (Hymenoptera: Formicidae)

2008 ◽  
Vol 140 (3) ◽  
pp. 312-323 ◽  
Author(s):  
Shumin Lü ◽  
Gengsi Xi ◽  
Xiaohui Wang
Keyword(s):  
Untranslated Region ◽  
Suppressor Gene ◽  
Base Pairs ◽  
Sequence Alignments ◽  
Reading Frame ◽  
Amino Acid Peptide ◽  
Late Instar ◽  
Males And Females ◽  
Polymerase Chain ◽  
Polyrhachis Vicina

AbstractQM, a tumor-suppressor gene, plays an important role in cell growth, differentiation, and apoptosis. In this report, a homologue of human QM was isolated from the ant Polyrhachis vicina Roger. The full-length cDNA of P. vicina QM (PvQM) is 827 base pairs (bp) and contains a 5′-untranslated region of 91 bp and a 3′-untranslated region of 77 bp. The open reading frame of PvQM encodes a deduced 219-amino acid peptide with a predicted molecular mass of 25.1 kilodaltons. The results of sequence alignments indicate that the PvQM protein shares an overall identity of 76.7%–98.2% with other known QM homologues, and is most closely related to that of Apis mellifera L. (Hymenoptera: Apidae). Real-time quantitative reverse transcription - polymerase chain reaction was performed to compare PvQM mRNA expression during P. vicina development and within different castes. The data revealed that PvQM mRNA is differentially expressed during P. vicina development, with the highest expression level in embryos and the lowest in late-instar larvae and pupae. The levels of PvQM transcripts also vary among castes, with higher levels in workers and lower levels in both males and females. These results suggest that PvQM is developmentally and caste-specifically regulated at the level of transcription.

Molecular cloning, characterization, and expression analysis of a novel sema-2a homologue in Polyrhachis vicina (Hymenoptera: Formicidae)

2010 ◽  
Vol 142 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Jing Luo ◽  
Geng-Si Xi ◽  
Shu-Min Lü ◽  
Ke Li ◽  
Qing Li
Keyword(s):  
Untranslated Region ◽  
Axonal Guidance ◽  
Mrna Levels ◽  
Chain Reaction ◽  
Base Pairs ◽  
Reading Frame ◽  
Acid Protein ◽  
Polymerase Chain ◽  
Polyrhachis Vicina ◽  
Amino Acid Protein

AbstractThe semaphorin gene family plays important roles in axonal guidance in vertebrates and invertebrates. Semaphorin 2a, a member of the semaphorin family, belongs to class 2, which is found only in invertebrates. In our study, semaphorin 2a was cloned from the ant Polyrhachis vicina Roger. The full length of P. vicina semaphorin 2a (Pv-sema-2a) is 2763 base pairs (bp) and it contains a 5′-untranslated region (UTR) 92 bp long and a 3′-UTR 521 bp long. The open reading frame of Pv-sema-2a encodes a 716-amino-acid protein with a predicted molecular mass of 81.1 kilodaltons. Real-time quantitative reverse-transcription – polymerase chain reaction indicated that Pv-sema-2a mRNA is differentially expressed during P. vicina development, in the whole bodies as well as the heads of different castes. The high mRNA levels in embryos and pupae suggest that Pv-sema-2a plays an important role in ant development.

scholarly journals Cloning, sequencing and expression of rat liver pyruvate carboxylase

1996 ◽  
Vol 316 (2) ◽  
pp. 631-637 ◽  
Author(s):  
Sarawut JITRAPAKDEE ◽  
Grant W. BOOKER ◽  
A. Ian CASSADY ◽  
John C. WALLACE
Keyword(s):  
Rat Liver ◽  
Pyruvate Carboxylase ◽  
Untranslated Region ◽  
Northern Analysis ◽  
Reading Frame ◽  
Liver Cdna Library ◽  
Lactating Mammary Gland ◽  
Polymerase Chain ◽  
Rapid Amplification ◽  
Sequencing And Expression

Overlapping clones encoding rat liver pyruvate carboxylase (PC) have been isolated by screening a liver cDNA library and by performing rapid amplification of cDNA ends polymerase chain reaction on total liver RNA. The sequence of rat PC cDNA contains an open reading frame of 3537 nucleotides encoding a polypeptide of 1178 amino acids with a calculated Mr of 129848. This is flanked by a 5′ untranslated region of 66 bp and a 3′ untranslated region of 421 bp including the poly(A) tail. The inferred protein sequence is 96.6% identical with mouse and 96.3% identical with human PCs, 68.4% identical with mosquito PC and 53.5% identical with yeast PC isoenzymes PC1 and PC2. On the basis of partial proteolysis and sequence homology with PC from other organisms (yeast, mosquito, mouse and human) and with other biotin enzymes, three functional domains, namely the biotin carboxylation domain, the transcarboxylation domain and the biotinyl domain, have been identified. Comparison with the known structure of the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase [Waldrop, Rayment and Holden (1994) Biochemistry 33, 10249–10256] highlights the functional importance of 11 highly conserved residues. Northern analysis revealed that PC mRNA is highly expressed in rat liver, kidney, adipose tissue and brain, moderately expressed in heart, adrenal gland and lactating mammary gland, and expressed at a low level in spleen and skeletal muscle.

scholarly journals Structure and Temperature Regulated Expression of a Cysteine Proteinase Gene in Pachysandra terminalis Sieb. & Zucc.

2007 ◽  
Vol 132 (1) ◽  
pp. 97-101
Author(s):  
Suping Zhou ◽  
Roger Sauve ◽  
Fur-Chi Chen
Keyword(s):  
Sequence Comparison ◽  
Cysteine Proteinase ◽  
Open Reading Frame ◽  
Chain Reaction ◽  
Base Pairs ◽  
Reading Frame ◽  
Conserved Motif ◽  
Regulated Expression ◽  
Polymerase Chain ◽  
Pro Region

A cysteine proteinase gene (DQ403257) with an open reading frame of 1125 base pairs was isolated from Pachysdandra terminalis. The primary translated peptide has a predicted length of 374 amino acids, pI (isoelectric point) of 5.70, and molecular mass of 40.9 kDa. The Peptidase_C1 domain is between residue 141 and 367. The proteinase has a conserved motif Gly-Xaa-Thy-Xaa-Phe-Xaa-Asn in the pro region. Sequence comparison shows that the deduced peptide shares 82% identity with the cysteine proteinase RD19a precursor (RD19) (accession P43296) from Arabidopsis thaliana (L.) Heynh. Real-time quantitative reverse-transcriptase–polymerase chain reaction revealed that the gene is induced by treatments of 1 to 7 days of darkness, 2 hours and 3 to 7 days at 5 °C, and 3 days at 38 °C.

Detection of the Glanzmann's Thrombasthenia Mutations in Arab and Iraqi-Jewish Patients by Polymerase Chain Reaction and Restriction Analysis of Blood or Urine Samples

1991 ◽  
Vol 66 (04) ◽  
pp. 500-504 ◽  
Author(s):  
H Peretz ◽  
U Seligsohn ◽  
E Zwang ◽  
B S Coller ◽  
P J Newman
Keyword(s):  
Polymerase Chain Reaction ◽  
Base Pair ◽  
Restriction Analysis ◽  
Urine Samples ◽  
Chain Reaction ◽  
Base Pairs ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia ◽  
Base Pair Deletion ◽  
Polymerase Chain

SummarySevere Glanzmann's thrombasthenia is relatively frequent in Iraqi-Jews and Arabs residing in Israel. We have recently described the mutations responsible for the disease in Iraqi-Jews – an 11 base pair deletion in exon 12 of the glycoprotein IIIa gene, and in Arabs – a 13 base pair deletion at the AG acceptor splice site of exon 4 on the glycoprotein IIb gene. In this communication we show that the Iraqi-Jewish mutation can be identified directly by polymerase chain reaction and gel electrophoresis. With specially designed oligonucleotide primers encompassing the mutation site, an 80 base pair segment amplified in healthy controls was clearly distinguished from the 69 base pair segment produced in patients. Patients from 11 unrelated Iraqi-Jewish families had the same mutation. The Arab mutation was identified by first amplifying a DNA segment consisting of 312 base pairs in controls and of 299 base pairs in patients, and then digestion by a restriction enzyme Stu-1, which recognizes a site that is absent in the mutant gene. In controls the 312 bp segment was digested into 235 and 77 bp fragments, while in patients there was no change in the size of the amplified 299 bp segment. The mutation was found in patients from 3 out of 5 unrelated Arab families. Both Iraqi-Jewish and Arab mutations were detectable in DNA extracted from blood and urine samples. The described simple methods of identifying the mutations should be useful for detection of the numerous potential carriers among the affected kindreds and for prenatal diagnosis using DNA extracted from chorionic villi samples.

scholarly journals Dendritic Transport and Localization of Protein Kinase Mζ mRNA

2004 ◽  
Vol 279 (50) ◽  
pp. 52613-52622 ◽  
Author(s):  
Ilham Aliagaevich Muslimov ◽  
Volker Nimmrich ◽  
Alejandro Ivan Hernandez ◽  
Andrew Tcherepanov ◽  
Todd Charlton Sacktor ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Translational Control ◽  
Untranslated Region ◽  
Functional Integration ◽  
Long Term Potentiation ◽  
Memory Storage ◽  
Reading Frame ◽  
Cis Acting ◽  
Translational Repressor ◽  
Protein Kinase Mζ

Protein kinase Mζ (PKMζ) is an atypical protein kinase C isoform that has been implicated in the protein synthesis-dependent maintenance of long term potentiation and memory storage in the brain. Synapse-associated kinases are uniquely positioned to promote enduring consolidation of structural and functional modifications at the synapse, provided that kinase mRNA is available on site for local input-specific translation. We now report that the mRNA encoding PKMζ is rapidly transported and specifically localized to synaptodendritic neuronal domains. Transport of PKMζ mRNA is specified by two cis-acting dendritic targeting elements (Mζ DTEs). Mζ DTE1, located at the interface of the 5′-untranslated region and the open reading frame, directs somato-dendritic export of the mRNA. Mζ DTE2, in contrast, is located in the 3′-untranslated region and is required for delivery of the mRNA to distal dendritic segments. Colocalization with translational repressor BC1 RNA in hippocampal dendrites suggests that PKMζ mRNA may be subject to translational control in local domains. Dendritic localization of PKMζ mRNA provides a molecular basis for the functional integration of synaptic signal transduction and translational control pathways.

Cloning of a gar (Lepisosteus osseus) GH cDNA: trends in actinopterygian GH structure

1996 ◽  
Vol 16 (1) ◽  
pp. 73-80 ◽  
Author(s):  
D A Rubin ◽  
J H Youson ◽  
L E Marra ◽  
R M Dores
Keyword(s):  
Cdna Library ◽  
Untranslated Region ◽  
Signal Sequence ◽  
Leader Sequence ◽  
Open Reading Frame ◽  
Russian Sturgeon ◽  
Reading Frame ◽  
Terminal Codon

ABSTRACT A cDNA containing the sequence of GH was cloned and sequenced from a pituitary cDNA library for the holostean fish Lepisosteus osseus (common name: gar). The gar GH cDNA contained an open reading frame of 633 nucleotides and a 3′ untranslated region (including the terminal codon TAG) of 1058 nucleotides. The overall length of the gar GH cDNA including leader sequence, signal sequence, hormone sequence and 3′ untranslated region was 1713 nucleotides. Thus, the gar GH cDNA is the largest vertebrate GH cDNA yet cloned. A comparison of GH sequences from ancient (holostean fishes — gar and bowfin; one chondrostean fish — the Russian sturgeon) and more modern (27 species of teleosts) members of class Actinopterygii indicate that members of this class have maintained many of the invariant residues deemed necessary for GH folding motifs (intramolecular relationships) observed in mammals.

scholarly journals One of the tightly clustered genes of the mouse surfeit locus is a highly expressed member of a multigene family whose other members are predominantly processed pseudogenes.

1988 ◽  
Vol 8 (9) ◽  
pp. 3898-3905 ◽  
Author(s):  
C Huxley ◽  
T Williams ◽  
M Fried
Keyword(s):  
Multigene Family ◽  
Open Reading Frame ◽  
The Other ◽  
Base Pairs ◽  
Regulation Of Expression ◽  
Reading Frame ◽  
Processed Pseudogenes ◽  
Dna Fragment ◽  
Basic Polypeptide

The mouse surfeit locus is unusual in that it contains a number of closely clustered genes (Surf-1, -2, and -4) that alternate in their direction of transcription (T. Williams, J. Yon, C. Huxley, and M. Fried, Proc. Natl. Acad. Sci. USA 85:3527-3530, 1988). The heterogeneous 5' ends of Surf-1 and Surf-2 are separated by 15 to 73 base pairs (bp), and the 3' ends of Surf-2 and Surf-4 overlap by 133 bp (T. Williams and M. Fried, Mol. Cell. Biol. 6:4558-4569, 1986; T. Williams and M. Fried, Nature (London) 322:275-279, 1986). A fourth gene in this locus, Surf-3, which is a member of a multigene family, has been identified. The poly(A) addition site of Surf-3 lies only 70 bp from the poly(A) addition site of Surf-1. Transcription of Surf-3 has been studied in the absence of the other members of its multigene family after transfection of a cloned genomic mouse DNA fragment, containing the Surf-3 gene, into heterologous monkey cells. Surf-3 specifies a highly expressed 1.0-kilobase mRNA that contains a long open reading frame of 266 amino acids, which would encode a highly basic polypeptide (23% Arg plus Lys). The other members of the Surf-3 multigene family are predominantly, if not entirely, intronless pseudogenes with the hallmarks of being generated by reverse transcription. The role of the very tight clustering on regulation of expression of the genes in the surfeit locus is discussed.

Expression of avian Ca2+-ATPase in cultured mouse myogenic cells

1989 ◽  
Vol 9 (5) ◽  
pp. 1978-1986
Author(s):  
N J Karin ◽  
Z Kaprielian ◽  
D M Fambrough
Keyword(s):  
Skeletal Muscle ◽  
Endoplasmic Reticulum ◽  
C2c12 Cells ◽  
Cyanine Dye ◽  
Adult Rabbit ◽  
Base Pairs ◽  
Reading Frame ◽  
Cytoplasmic Vesicles ◽  
Fast Twitch ◽  
Chicken Skeletal Muscle

cDNA encoding Ca2+-ATPase was cloned from a chicken skeletal muscle library. The cDNA (termed FCa) comprised 3,239 base pairs, including an open reading frame encoding 994 amino acids which showed the highest degree of homology with the adult rabbit fast-twitch Ca2+-ATPase isoform (C. J. Brandl, S. de Leon, D. R. Martin, and D. H. MacLennan, J. Biol. Chem. 262:3768-3774, 1987). Radiolabeled FCa hybridized to a 3.2-kilobase transcript in chicken skeletal muscle RNA but not to cardiac muscle RNA, which confirmed its identity as encoding the fast Ca2+-ATPase isoenzyme. FCa was transfected into the mouse myogenic line C2C12, from which a protein of 100 kilodaltons was immunopurified by using a monoclonal antibody specific for the avian fast Ca2+-ATPase. Immunofluorescence microscopy of a line (designated C2FCa2) stably expressing the avian Ca2+-ATPase localized the protein to the nuclear envelope and a population of cytoplasmic vesicles. A similar pattern was observed when C2FCa2 cells were stained with DiOC6(3), a cyanine dye that labels endoplasmic reticulum and mitochondria (M. Terasaki, J. Song, J. R. Wong, M. J. Weiss, and L. B. Chen, Cell 38:101-108, 1984). We conclude that the avian Ca2+-ATPase fast isoform is expressed and correctly targeted to the endoplasmic reticulum in mouse C2C12 cells.

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