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PubMed2002

Successful inactivation of endogenous Oct-3/4 and c-mos genes in mouse preimplantation embryos and oocytes using short interfering RNAs.

Understanding oocyte maturation and early development in mammals is very important, especially because these cells serve as a source of materials useful in medical applications, such as ES cells. However, the limited availability of oocytes and embryos hampers the molecular dissection of the very early stage of mammalian development. Recently, the RNA interference technology has been acknowledged to be very effective and useful in diverse groups of cells, including mammalian cells. In this study, we examined whether short interfering RNAs (siRNAs) are applicable to mouse oocytes and preimplantation embryos, by targeting two genes, namely, Oct-3/4 and c-mos. siRNA injections successfully extinguished the production of these target genes. Moreover, the siRNA-injected oocytes and embryos showed phenotypes very similar to those exhibited by Oct-3/4- or Mos-knockout mice in previous studies. Accordingly, we concluded that siRNA is a useful tool in molecular studies on the early development of mouse.

Alkaline Phosphatase↗
PubMed1982

Human DNA sequence homologous to the transforming gene (mos) of Moloney murine sarcoma virus.

We describe the molecular cloning of a 9-kilo-base-pair BamHI fragment from human placental DNA containing a sequence homologous to the transforming gene (v-mos) of Moloney murine sarcoma virus. The DNA sequence of the homologous region of human DNA (termed humos) was resolved and compared to that of the mouse cellular homolog of v-mos (termed mumos) [Van Beveren, C., van Straaten, F., Galleshaw, J.A. & Verma, I.M. (1981) Cell 27, 97-108]. The humos gene contained an open reading frame of 346 codons that was aligned with the equivalent mumos DNA sequence by the introduction of two gaps of 15 and 3 bases into the mumos DNA and a single gap of 9 bases into the humos DNA. The aligned coding sequences were 77% homologous and terminated at equivalent opal codons. The humos open reading frame initiated at an ATG found internally in the mumos coding sequence. The polypeptides predicted from the DNA sequence to be encoded by humos and mumos also were found to be extensively homologous, and 253 of 337 amino acids were shared between the two polypeptides. The first five NH2-terminal and last two COOH-terminal amino acids of the humos gene product were in common with those of mumos. In addition, near the middle of the polypeptide chains, four regions ranging from 19 to 26 consecutive amino acids were conserved. However, we have not been able to transform mouse cells with transfected humos DNA fragments or with hybrid DNA recombinants containing humos and retroviral long terminal repeat (LTR) sequences.

Animals↗
PubMed1991

The c-mos gene product is required for cyclin B accumulation during meiosis of mouse eggs.

The c-mos protooncogene is expressed as a maternal message that is required for oocyte meiosis. The mechanism of action of c-mos was investigated by analysis of mouse eggs injected with antisense c-mos oligonucleotides. In antisense-injected eggs, maturation-promoting factor was not reactivated after the completion of meiosis I, leading to the formation of nuclei containing decondensed chromatin within 2-3 hr after polar body extrusion. This was correlated with a failure of the injected eggs to accumulate newly synthesized cyclin B. The c-mos protooncogene thus appears to affect the pathway that regulates cyclin B stability during meiosis of mouse eggs.

Animals↗
PubMed1987

Localization of the human c-mos gene by in situ hybridization in two cases of acute nonlymphocytic leukemia type M2.

The t(8;21)(q22.1;q22.3) is specific for the FAB-M2 subtype of acute nonlymphocytic leukemia (ANLL). The human c-mos protooncogene is located near the site of rearrangement on chromosome #8, at a position corresponding to band 8q22. The present in situ hybridization studies were performed in order to establish if c-mos is transposed from chromosome #8 to chromosome #21, in two cases of M2-ANLL showing the typical t(8;21). A statistical analysis of the results revealed that the c-mos oncogene was definitely not translocated from chromosome #8 to #21 in one of these patients, and was inconclusive in the other patient. The findings in the former patient suggest that either c-mos is not involved in the etiology of M2-ANLL or, alternatively, if c-mos is important in the pathogenesis of this disease, it must be activated by some mechanism other than transposition of this oncogene to an aberrant position.

Acute Disease↗
PubMed1989

Translocation of the MOS gene in a rare t(8;16) associated with acute myeloblastic leukemia and Down syndrome.

Cytogenetic analysis of an infant with Down syndrome with concomitant acute myelogenous leukemia revealed a unique t(8;16)(q22;q24). In situ chromosomal hybridization was used to demonstrate that the protooncogene MOS was translocated from chromosome 8 to chromosome 16. This is the first report of the transposition of MOS in association with acute leukemia.

Chromosomes, Human, Pair 16↗
PubMed1986

Monoclonal antibody detection of transformation associated protein (TAP) in ts110 Moloney murine sarcoma virus transformed 6M2 cells that are different from the mos gene product.

By the use of a highly specific monoclonal antibody (designated MC), we were able to detect three radiolabeled bands with molecular weights of 60,000, 63,000, and 66,000 daltons in the ts-110 Moloney murine sarcoma virus mutant-transformed rat kidney cells known as 6M2. Expression of transformation properties as well as these three bands in 6M2 cells was found to be temperature sensitive. Therefore, MC detected factors that are apparently associated with the transformation of 6M2 cells. These factors are tentatively referred to as transformation associated proteins. These transformation proteins were found in two other Moloney murine sarcoma virus-transformed rat cell lines. These proteins were found to differ from known gene products of the ts-110 Moloney murine sarcoma virus mutant and do not have kinase activity. The transformation associated proteins may represent rat cellular factors activated during the transformation of rat cells by Moloney murine sarcoma virus.

Animals↗
PubMed1991

Production and characterization of a monoclonal antibody to the v-mos oncogene protein.

Valuable information about proto-oncogenes and their physiological functions has been obtained by studying their expression in normal cells. However, the protein product of the c-mos gene, the cellular homologue of the transforming gene (v-mos) of Moloney murine sarcoma virus, has not been detected in normal mouse cells or tissues. Here, we have constructed a v-mos expression vector, pRI-delta mos, which directs the synthesis of a truncated v-mos gene product, a protein A fusion protein. Using the truncated v-mos oncoprotein produced in Escherichia coli as immunogen, we prepared anti-v-mos monoclonal antibodies (MAbs). In immunoblotting assays, the MAb was reactive with v-mos oncoprotein and detected bands at 43 KDa or 39 kDa in the tissue extract of mouse testes or ovaries, respectively, in which the c-mos protooncogene mRNA is expressed. These results demonstrate that the v-mos MAb obtained is suitable for elucidating the physiological functions of v-mos gene product and may also be utilized to detect c-mos gene product at the cellular level.

Animals↗
PubMed2004

[The use of c-mos nuclear gene as a phylogenetic marker in tetraonidae birds].

A 480-bp fragment of nuclear c-mos gene was sequenced in nine bird species representing four genera of the family Tetraonidae. It was demonstrated that nuclear genome region examined was highly conservative. The data were used to construct phylogenetic relationships among the c-mos gene sequences in Tetraonidae. The data obtained point to a paraphyletic origin of hazel grouse (Bonasa bonasia) and ruffed grouse (Bonasa umbellus).

Animals↗
PubMed1985

[Regions of the human genome containing homologs of the oncogenes and retrovirus genes. 3. The primary structure of the mos-related region CL-1 from the ORAgp5 locus].

The nucleotide sequence of 686 bp from the cloned human genome locus gp5 has been determined. Analysis of this sequence has revealed a statistically significant homology with both the viral and murine mos genes. The region of mos homology contains two adjacent homologous domains, whereas their counterparts in viral mos gene are separated by 471 bp. The position of mos homologous region in the close vicinity to LTR of endogenous human viral-like repeat is in accordance with the hypothesis of retroviral involvement in the process of mos gene amplification.

Base Sequence↗
PubMed1987

The P55 protein affected by v-mos expression is vimentin.

Rabbit antiserum prepared against a cyclic 19-amino-acid peptide predicted from the sequence of the viral mos gene (v-mos) of Moloney murine sarcoma virus not only recognized v-mos gene products but also specifically detected a 55,000-Mr polypeptide expressed in a variety of cells that grow on solid surfaces. This normal cellular protein, previously shown to be reduced in amount in cells expressing the v-mos gene, was found to be the intermediate filament structural protein, vimentin. This conclusion was reached by comparing relative mobilities in denaturing gels, isoelectric points, immunoreactivities, location in the cell, and peptide maps.

Animals↗
PubMed1992

v-mos proteins encoded by myeloproliferative sarcoma virus and its ts159 mutant.

The myeloproliferative sarcoma virus (MPSV) v-mos protein was predicted to be identical in size to p39c-mos because of an observed one-base deletion in the seventh codon of the env-mos open reading frame, which would allow translation to initiate at the methionine equivalent to codon 32 of the env-mos gene. On the basis of published results, p39c-mos is known to have greatly reduced in vitro protein kinase activity compared with p37env-mos encoded by Moloney murine sarcoma virus. Unexpectedly, the relative activity of the MPSV v-mos protein kinase was comparable to that of p37env-mos. Consistent with this finding, the size of MPSV v-mos protein was found to be similar to the size of p37env-mos. Moreover, the pattern and sizes of phosphorylated bands produced by autophosphorylation of the MPSV v-mos protein were similar to those of p37env-mos. These results were confirmed by in vitro transcription-translation of the MPSV v-mos gene. Resequencing portions of the MPSV mos gene failed to show the deletion within codon 7. Except for the codon 262 deletion, other mutations characteristic of MPSV and temperature-sensitive MPSV v-mos genes were confirmed. A glycine-to-arginine mutation at residue 338 of the MPSV env-mos sequence, previously shown to cause thermosensitivity of the mutant virus (termed ts159) transforming function, yielded a v-mos protein that had significantly reduced protein kinase activity in vitro. These findings indicate that MPSV, like other Moloney murine sarcoma virus strains, also encodes a functional env-mos protein.

Amino Acid Sequence↗
PubMed1990

v-mos protein produced by in vitro translation has protein kinase activity.

The v-mos protein, termed p37v-mos, has a closely associated serine/threonine protein kinase activity. To provide further information about its protein kinase activity, we tested the activity of p37v-mos produced in a cell-free translation system from transcripts generated from a cloned v-mos gene. Anti-mos(37-55) immunoprecipitates of in vitro-produced p37v-mos were found to possess serine/threonine protein kinase activity, whereas those obtained with anti-mos(260-271), known to block v-mos autophosphorylation, lacked kinase activity. The phosphorylated products were identical in size to p37v-mos and p43v-mos produced in protein kinase assays from Moloney murine sarcoma virus-infected cells expressing authentic p37v-mos. These results provide further proof that the protein kinase activity associated with p37v-mos is an intrinsic property of the v-mos gene product. This translation system also provides a useful experimental model to study the activation of the mos protein kinase. Thus, protein kinase assays performed on [35S]methionine-labeled p37v-mos produced p43v-mos at the expense of p37v-mos. Phosphatase treatment removed the p43v-mos species, resulting in increase of the p37v-mos-sized protein, confirming our previous interpretation that p43v-mos is a hyperphosphorylated form of p37v-mos.

Animals↗
PubMed1988

Increased amount of a 25-kilodalton phosphoprotein after v-mos transfection of CHO cells.

We transfected Chinese hamster ovary (CHO) cells with a cloned v-mos gene (pHT25). The mos family of oncogenes has previously been shown to have serine-threonine kinase activity. This kinase activity may be required for oncogenic transformation, although its exact biological role is unknown. We found that the transfected cells had an altered morphology, a slower doubling time, and an apparent increase in the amount of a 25-kilodalton (kDa) phosphoprotein that appeared to be of low abundance. Transfection of CHO cells with a cloned temperature-sensitive mos gene (ts159) led to isolation of a cell line that showed the presence of the 25-kDa phosphoprotein at the permissive but not at the nonpermissive temperature, suggesting a direct relationship between mos activity and the presence of this phosphoprotein. The characteristics of altered morphology and depressed growth rate were reminiscent of changes seen after the activation of the cyclic AMP-dependent protein kinase (PKA) in CHO cells. However, PKA activation did not stimulate phosphorylation of this 25-kDa protein, nor was there a change in total PKA activity in these cells. We suggest that the increased presence of the 25-kDa phosphoprotein is a consequence of the v-mos transfection and that it may be involved in the change of morphology and growth rate seen in the CHO cells. Phosphorylation of this protein may be a useful marker of mos and have some functional importance in the transformation of cells by the v-mos oncogene.

Animals↗
PubMed1982

Moloney murine leukemia virus-induced tumors: recombinant proviruses in active chromatin regions.

The DNase I sensitivity of chromosomal DNA regions carrying integrated proviral genomes of Moloney (M-MuLV) and AKR Murine Leukemia Virus (AKR-MuLV), and the cellular homologue of the mos-gene (c-mos) of Moloney Sarcoma Virus (MSV) were studied in tumor tissues of leukemic mice. The genetically transmitted sequences of M-MuLV, AKR-MuLV, and the c-mos gene are all in DNase I resistant chromatin conformations in M-MuLV-induced tumors. Each M-MuLV-induced tumor contained at least one somatically acquired integrated recombinant MuLV genome that displayed two main characteristic features of active chromatin: a) a configuration hypersensitive to DNase I, and b) extensive hypomethylation. DNase I hypersensitive sites were mapped at the junction of cellular sequences and the 5'-viral large terminal repeat (LTR). Expression of a recombinant MuLV seems therefore to be a necessary feature to maintain the transformed state.

AKR murine leukemia virus↗
PubMed1992

Evidence for interaction between v-Mos and a p34cdc2 isoform, p35cdk.

The c-mos gene product (c-Mos) encodes a serine/threonine kinase required for activation of pre-MPF (maturation-promoting factor) to MPF in oocytes undergoing meiosis and also for stabilization of MPF leading to metaphase arrest in unfertilized eggs. In order to determine whether the v-mos gene product (v-Mos) causes neoplastic transformation via interaction with cell cycle control elements, we have searched for proteins that interact with v-Mos. Extracts of NIH3T3 cells transformed by v-Mos encoded by Moloney murine sarcoma virus (Mo-MuSV) were examined by gel filtration, by immunoprecipitation with antibodies to a conserved region of p34cdc2, and by binding to beads that contain cross-linked p13suc1, a protein known to bind p34cdc2. Gel filtration detected a 500-kDa complex that contained v-Mos and a p34cdc2 isoform, termed p35cdk. The 500-kDa macromolecular complex also exhibited histone H1 phosphorylation activity, consistent with the presence of a cdc2 isoform. The identity of p35cdk is based on its recognition by anti-cdc2 PSTAIR but not by anti-cdc2 C-terminal antibodies, which detect authentic p34cdc2. Structures containing v-Mos and p35cdk were also detected by experiments involving co-immunoprecipitation of v-Mos with anti-cdc2 PSTAIR antibodies. Furthermore, both v-Mos and the p35cdk co-precipitated with p13suc1-Sepharose beads. Our findings raise the possibility of a v-Mos-p35cdk regulatory interaction in cells transformed by Mo-MuSV.

3T3 Cells↗
PubMed1987

Genes for the catabolism and synthesis of an opine-like compound in Rhizobium meliloti are closely linked and on the Sym plasmid.

In alfalfa nodules induced by Rhizobium meliloti strain L5-30 the compound L-3-O-methyl-scyllo-inosamine (3-O-MSI) is synthesized. This compound is also catabolized specifically by this strain. Its biological properties are therefore similar to the Agrobacterium opines. To answer the question whether opine-like compounds ("Rhizopines") play a role in a plant symbiotic interaction, we isolated the genes for the catabolism of 3-O-MSI (moc genes) and for the induction of its synthesis in the nodule [mos gene(s)]. moc and mos genes were shown to be closely linked and located on the Sym plasmid of L5-30, suggesting that they have co-evolved and may be important in symbiosis. These genes have been cloned into a broad host-range vector that can be mobilized into other R. meliloti strains where they are expressed. The location of the mos genes in the bacteria extends the opine concept, initially developed for a plant pathological interaction, to a symbiotic one.

Journal Article↗