Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Library preparation”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,099 records · Page 61Linked to original sources
PubMed1994

Cloning and sequencing of rat kidney L-arginine:glycine amidinotransferase. Studies on the mechanism of regulation by growth hormone and creatine.

L-Arginine-glycine amidinotransferase (transamidinase) is the first and rate-limiting step in creatine biosynthesis. Rats fed a creatine-supplemented diet or hypophysectomized rats have only 20% of the kidney transamidinase activity as intact rats fed a creatine-free diet. A cDNA clone corresponding to transamidinase was isolated by immunoscreening of a lambda gt11 expression library prepared from rat kidney mRNA. The transamidinase cDNA had an open reading frame containing the known sequence of the amino-terminal peptide of transamidinase. Based on the cDNA sequence, transamidinase is synthesized as a precursor with an amino-terminal extension of 50 amino acids, consistent with its mitochondrial localization. Comparison of the transamidinase sequence with the protein data base identified only a single, related protein. Remarkably, this protein, which has a 37% amino acid identity with transamidinase, is also an amidinotransferase, catalyzing streptomycin biosynthesis in Streptomyces griseus. Transamidinase cDNA was used to investigate the regulation of mRNA levels by creatine and growth hormone. Hypophysectomized rats were fed a creatine-free or a creatine-supplemented diet and maintained with and without injections of growth hormone. An excellent correlation was found between changes in transamidinase activity and mRNA levels in response to creatine and growth hormone. Thus, the regulation of transamidinase by creatine and growth hormone is at a pretranslational level. In addition, the two effectors do not act independently but interact at a pretranslational level to control transamidinase gene expression.

Amidinotransferases↗
PubMed1994

Commonality of the gene programs induced by effectors of apoptosis in androgen-dependent and -independent prostate cells.

Prostate tissue is composed of both androgen-dependent and -independent cells. To identify the gene program induced by effectors of apoptosis in both of these cell types, we performed differential hybridization on a complementary DNA library prepared from an androgen-independent prostate cancer cell line, AT-3, exposed to ionomycin. Five distinct complementary DNAs representing ionomycin-inducible genes, designated prostate apoptosis response (par) -1, -2, -3, -4, and -5, were identified. Nucleotide sequencing identified par-1 as the rat homologue of a serum- and oxidative stress-inducible gene, 3CH134/erp/CL100; par-2 as the injury-inducible gene HB-EGF encoding a heparin-binding epidermal growth factor-like growth factor; par-3 as the serum-inducible gene cyr-61; whereas par-4 and par-5 were novel, as judged by a GenBank search. par-1, -3, -4, and -5 were also induced in rat ventral prostate following castration, which causes androgen ablation, leading to apoptosis of androgen-dependent prostate cells. Pretreatment of rats with nifedipine prior to castration abrogated inducible expression of the par genes, indicating that their expression was downstream to Ca2+ elevation. Further characterization of these genes revealed that induction of par-4 is apoptosis specific: it is not induced by effectors of growth stimulation, oxidative stress and necrosis, or growth arrest in prostate cells. Together, par-1, -3, -4, and -5 represent an apoptosis response gene program common to both androgen-dependent and -independent prostate cells. Thus, cell death programs in prostate cells are comprised of genes specifically associated with apoptosis as well as those with multifunctional roles in growth regulation. Since elevation of intracellular Ca2+ is central to apoptosis in many cell types, we predict that par genes will be important components of diverse effector-driven apoptotic pathways.

Androgens↗
PubMed1994

Cloning and sequence analysis of the promoter region of the MRP gene of HL60 cells isolated for resistance to adriamycin.

Non-P-glycoprotein multidrug resistance of HL60/ADR cells appears to be related to overexpression of the MRP gene. Recent studies suggest that this gene may play an important role in a new form of cell resistance to certain chemotherapeutic agents. To examine mechanisms regulating transcriptional activity of this gene, a 2.2-kilobase 5'-flanking sequence of MRP has been isolated from a genomic library prepared from HL60/ADR cells. The 2.2-kilobase DNA fragment linked to the chloramphenicol acetyltransferase (CAT) gene in a reporter plasmid was found to be capable of driving expression of this gene in transient transfection experiments. This DNA containing promoter activity has been sequenced in its entirety and found to contain multiple putative regulatory sites. A series of deletion mutants linked to the CAT reporter gene was used to examine functional domains of the 2.2-kilobase sequence. The results suggest that promoter activity is contained in nucleotides -91 to +103 in a GC-rich region of the MRP genome. Promoter activity contained within this sequence, however, is modulated by both positive and negative regulatory elements. Certain of the regulatory sites contain consensus sequences for positive and negative regulatory elements which have been found in the promoter regions of other genes. Primer extension analysis indicates the presence of multiple major transcriptional start sites from the MRP promoter. Sequence analysis of MRP genomic and complementary DNAs has defined the exon/intron boundaries and the organization of a portion of the 5'-end region of the MRP genome. The results of these studies thus provide new insight in site-specific domains which may function in the regulation of MRP gene expression.

Base Sequence↗
PubMed1994

Isolation, cloning, and characterization of new chitinase stored in active form in chitin-lined venom reservoir.

A 52-kDa protein was purified from the venom gland of an endoparasitic wasp Chelonus sp. near curvimaculatus. The acidic protein (pl 4.8-5.0) was purified, and the NH2-terminal amino acid sequence was determined by direct protein sequencing. A vector-anchored primer and a degenerate primer derived from an 8-amino acid region of the NH2 terminus were used in anchored polymerase chain reaction to generate a probe for screening a cDNA library prepared from mRNA from the venom gland of this wasp. A positive clone of 1596 nucleotides was isolated, sequenced, and found to contain an open reading frame encoding a protein of 483 amino acids. The amino acid sequence encoded in the cDNA clone at the amino terminus was identical to the sequence determined from the purified 52-kDa protein. Comparison of the inferred protein sequence against all of the sequences in the GenBank data base revealed a high degree of similarity to a 62-kDa insect chitinase that is expressed at each molt for the purpose of digesting the chitinous insect cuticle. Two regions that are conserved in a group of chitinases from insects, bacteria and fungi, were also conserved in the wasp 52-kDa protein. The region between amino acid residues 382 and 464 in the 52-kDa wasp chitinase markedly differed in primary sequence from the corresponding region in the 62-kDa insect chitinase, although this region in both the proteins is predicted to have a similar secondary structure predominantly of coils and turns. This region may impart unique structural properties to the 52-kDa chitinase that enables it to exist in an active form in a chitin-lined reservoir without exerting an autotoxic effect to digest the cuticular storage reservoir. Chitinolytic activity occurring in the total venom gland extract was kinetically indistinguishable from that observed for the purified 52-kDa protein, including the substrate concentrations at which maximal velocity and substrate inhibition were reached. The kinetic properties of the 52-kDa wasp chitinase were quite distinct from Serratia marcescens chitinase for both catalytic rate and substrate inhibition.

Amino Acid Sequence↗
PubMed1994

Molecular cloning and characterization of a murine LPS-inducible cDNA.

Murine macrophages respond to endotoxins by inducing a vast array of genes that play a major role in the host's response to infection and tumor growth. We have isolated and characterized a 1.8-kb cDNA, designated IRG2, from a cDNA library prepared from RNA isolated from the murine cell line, RAW 264.7, after bacterial LPS stimulation. The cDNA encodes a protein of 47 kDa that is the murine homologue of a small family of proteins described from IFN-induced human cells. The IRG2 message does not appear until 3 h after LPS exposure and its induction is dependent on new protein synthesis. IRG2 induction by LPS is slightly inhibited by the anti-inflammatory steroid, dexamethasone. Increasing cytosolic cAMP with either forskolin, dibutyryl cAMP, or 8-(4-chlorophenylthio)-cAMP caused marked inhibition of the LPS induction of IRG2. In contrast, activation of PKC with phorbol ester potentiated the LPS response. Removing extracellular Ca2+ with EGTA inhibited IRG2 induction; increasing intracellular calcium with the calcium ionophore A23187 led to enhanced levels of the IRG2 transcript. These data suggest that the induction of IRG2 occurs via a PKC pathway.

Amino Acid Sequence↗
PubMed1993

A cDNA clone encoding the mouse Qa-1a histocompatibility antigen and proposed structure of the putative peptide binding site.

We have isolated a cDNA clone which encodes the Qa-1a histocompatibility Ag from a library prepared from Con A-activated B10.BR mouse spleen cells. The clone encodes a protein of 322 amino acids with three potential N-glycosylation sites. The coding sequence shows strongest similarity with that of the T23d gene of DBA/2 mice which encodes the Qa-1b molecule. Molecular modeling of the putative peptide-combining site indicates most of the differences between Qa-1a and Qa-1b are located peripheral to the binding cleft, with only two amino acid substitutions, at positions 9 and 24, which might affect peptide binding. Many features of the Qa-1 binding cleft are also conserved in the rat RTBM.1 and in human HLA-E molecules. This suggests that all of these molecules may associate with structurally similar peptides.

Amino Acid Sequence↗
PubMed1993

TSG-6: a TNF-, IL-1-, and LPS-inducible secreted glycoprotein associated with arthritis.

TSG-6 (TNF-stimulated gene 6) was originally discovered by differential screening of a cDNA library prepared from TNF-stimulated human diploid FS-4 fibroblasts. We show that the 35-kDa protein encoded by TSG-6 was undetectable in the medium of untreated FS-4 cultures, whereas its production reached approximately 1400 and 700 ng/10(6) cells after 24-h treatment with IL-1 or TNF, respectively. Stimulation of TSG-6 protein and mRNA levels was also demonstrated in normal human mononuclear cells by treatment with TNF and, especially, by LPS. In view of the inducibility of TSG-6 by inflammatory cytokines and its earlier demonstrated affinity for hyaluronan, we examined the presence of TSG-6 protein in the synovial fluids from patients with various forms of arthritis. TSG-6 protein was undetectable in the joint fluids of persons with no known history of arthritis, but high levels of TSG-6 oere demonstrated in the synovial fluids of a majority of arthritis patients. TSG-6 protein was also detected in the sera of some of the arthritis patients, albeit at concentrations that were less than in the joint fluids. To investigate the source of TSG-6 in the synovial fluids, we examined the production of TSG-6 protein in cultures of synovial cells. Synoviocytes from rheumatoid arthritis patients produced TSG-6 protein constitutively, and this production was increased by treatment with TNF or IL-1, but not with TGF-beta. Steady-state levels of TSG-6 mRNA were also increased in synoviocytes after treatment with TNF or IL-1. The presence of high levels of TSG-6 protein in the synovial fluids of arthritis patients and its inducibility by inflammatory cytokines in fibroblasts, mononuclear cells, synoviocytes, and chondrocytes suggest a role for TSG-6 in arthritis and inflammation.

Adolescent↗
PubMed1994

Structural analysis of the chicken max gene.

The recent identification of Max, a nuclear phosphoprotein that dimerizes with members of the Myc protein family, has provided an additional tool to examine the role of the Myc oncoprotein as a sequence-specific DNA binding protein and a potential regulator of gene transcription. Here we report the nucleotide sequence of an avian max gene isolated from a lambda EMBL3 genomic library prepared from size-selected chicken embryo fibroblast DNA. The complete transcription unit encoding chicken Max is contained on a 5.7 kbp BglII DNA fragment which expresses an appropriately sized max mRNA of 1.5 kb following transfection of C3H10T1/2 mouse fibroblasts. The coding region of the chicken max gene is organized into five exons and the overall identity between the human and chicken max coding sequences is 85% at the nucleotide level and 96% at the amino acid level. The basic helix-loop-helix/leucine zipper region, the casein kinase II phosphorylation sites and the nuclear localization signal sequence are 100% conserved in all vertebrate Max proteins characterized to date. DNA sequence analysis of the 5' flanking region of the chicken max coding sequence reveals the absence of consensus TATA or CAAT motifs, but the presence of numerous GC-rich sequences that are typical in eukaryotic genes which are expressed constitutively in different tissues and under different growth conditions.

Amino Acid Sequence↗
PubMed1994

Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts.

Three complete cDNA clones encoding Id-related helix-loop-helix (HLH) proteins lacking a basic region were isolated from a pcD2 cDNA expression library prepared from TIG-3 human diploid fibroblasts (HDF). Of these cDNAs (Id-1H, Id-1H', and Id-2H), two (Id-1H and Id-1H') appeared to be derived by alternative RNA splicing. Id-1H and Id-2H seem to be human homologues of mouse Id-1 and Id-2, respectively, and have potential to encode 154 and 135 amino acid proteins. The Id-1H and Id-2H mRNAs were barely detectable in quiescent early passage HDF; serum coordinately induced both mRNAs, with two peaks of expression, in early and late in G1. Antisense oligomers complementary to Id-1H and Id-2H mRNA prevented early passage HDF from entering the S phase of the cell cycle. The treatment of serum-stimulated early passage cells with the antisense Id-1H oligomer completely abolished Id-1H. In senescent cells, serum barely induced the Id-1H and Id-2H mRNAs, although the levels of c-myc expression induced were similar in early passage and senescent cells. The expression levels of these Id genes vary among immortal human cell lines. Both genes were overexpressed in VA4 SV40-transformed lung fibroblasts and EJ-1 bladder carcinoma cells, while these genes were expressed at a very low level in SVts8 cells derived from SV40 tsA-transformed TIG-3 cells. SVts8 cells may acquire some function redundant to Id proteins. HT1080 fibrosarcoma cells expressed the Id-1H gene but not the Id-2H gene, suggesting these Id genes may subserve redundant functions.

Alternative Splicing↗
PubMed1993

A novel putative receptor protein tyrosine kinase of the met family.

By successive screenings of cDNA libraries prepared from human tumours and from human foreskin keratinocytes, we have isolated overlapping cDNAs coding for a novel protein which we call Ron, with sequence characteristics of a receptor protein tyrosine kinase. Ron is a 1400 amino acid protein structurally similar to the 1408 amino acid product of the C-MET proto-oncogene, the receptor for hepatocyte growth factor and scatter factor. The two proteins have 63% overall sequence identity in their intracellular regions. We have localised the RON gene to human chromosome region 3p21, a region frequently deleted in small cell carcinoma of the lung and in renal cell carcinoma, and which is believed to harbour unidentified tumour suppressor genes. Interestingly, normal lung tissue contains transcripts of the RON gene.

Amino Acid Sequence↗
PubMed1993

A serine/proline-rich protein is fused to HRX in t(4;11) acute leukemias.

Translocations involving chromosome band 11q23 in acute leukemias have recently been shown to involve the HRX gene that codes for a protein with significant similarity to Drosophila trithorax. HRX gene alterations are consistently observed in t(4;11) (q21;q23)-carrying leukemias and cell lines by Southern blot analyses and are accompanied by HRX transcripts of anomalous size on Northern blots. HRX-homologous cDNAs were isolated from a library prepared from t(4;11)-carrying acute leukemia cells. cDNAs representative of transcription products from the derivative 11 chromosome were shown to contain HRX sequences fused to sequences derived from chromosome band 4q21. Fragments of the latter were used to clone and analyze cDNAs for wild-type 4q21 transcripts that predicted a 140-Kd basic protein (named FEL) that is rich in prolines, serines, and charged amino acids. FEL contains guanosine triphosphate-binding and nuclear localization consensus sequences and uses one of two possible 5' exons encoding the first 12 or 5 amino acids. After t(4;11) translocations, 913 C-terminal amino acids of FEL are fused in frame to the N-terminal portion of HRX containing its minor groove DNA binding motifs. These features are similar to predicted t(11;19) fusion proteins, suggesting that HRX consistently contributes a novel DNA-binding motif to at least two different chimeric proteins in acute leukemias.

Amino Acid Sequence↗
PubMed1993

Hexokinase II mRNA and gene structure, regulation by insulin, and evolution.

A DNA segment that is highly conserved in glucokinase (hexokinase IV) and hexokinase I cDNA was used to identify specific cDNAs in a library prepared from rat adipose tissue mRNA. Some of these cDNAs were identified as being hexokinase I cDNA. Others, although similar to both the glucokinase and hexokinase I cDNAs, were unique. Two of these unique cDNAs overlapped and contained an open reading frame that encoded a protein of 103 kDa which, when expressed in Escherichia coli, had kinetic properties characteristic of hexokinase II. The entire hexokinase II mRNA sequence and the exon-intron structure of the hexokinase II gene were determined. A single transcription initiation site and two distinct termination sites account for the two observed hexokinase II RNA species of 5500 and 4400 nucleotides that were detected when either of the cDNAs was used as a hybridization probe against poly(A)+ RNA isolated from rat adipose tissue. Hexokinase II mRNA was decreased in adipose tissue from diabetic rats, but was restored by insulin treatment to levels found in nondiabetic control rats. Insulin also induced hexokinase II mRNA in two adipose cell lines (3T3-F442A and BFC-1B) and two skeletal muscle cell lines (C2C12 and L6). In L6 cells, this increase was accounted for by a corresponding increase of hexokinase II gene transcription. Comparison of the structures of the hexokinase II and glucokinase genes support the hypothesis that the 100-kDa hexokinase arose by gene duplication and tandem ligation of a 50-kDa glucokinase-like ancestral gene.

Adipose Tissue↗
PubMed1995

[Negative repressor THZif-1 of protooncogene c-myc].

A human recombinant cDNA clone that encoded 253 amino acids residues of a zinc-finger protein (THZif-1) was cloned by screening a cDNA library prepared from human promyelocytic leukemia HL60 cells with synthetic oligodeoxynucleotide probes that corresponded to the amino acid sequences of tryptic peptides derived from the DNA-binding protein specific for the nuclease-hypersensitive element (NHE) of the human c-myc gene. The predicted amino acid sequence of THZif-1 included a DNA-binding domain that contained five tandemly repeated zinc finger motifs. The three amino-terminal sets of zinc finger motifs, including the second finger, were found to be responsible for high-affinity interactions with the triple-helical conformation of NHE, as well as for high-affinity binding to the single-pyrimidine-rich strand of NHE in a sequence-specific manner. Cotransfection, trans-activation and in vitro transcription studies using the wild-type form and THZif-1 with a mutated second zinc finger motif demonstrated that the DNA-binding activity specific for H-form DNA of NHE was a prerequisite for the negative regulation of the expression of the c-myc gene.

Amino Acid Sequence↗
PubMed1996

Determinants of polyreactivity in a large panel of recombinant human antibodies from HIV-1 infection.

A considerable part of the Ab repertoire is given over to polyreactive Abs capable of interacting with multiple antigenic species. Neither the function of these Abs nor the molecular basis for their activity is known. To address the latter problem, we have compared the amino acid sequences of a large panel (n = 70) of polyreactive human monoclonal Fab fragments and conducted a series of engineering experiments on a prototype polyreactive Fab. The Fab fragments were retrieved from combinatorial IgG libraries prepared from the bone marrow of long term asymptomatic HIV-1 seropositive donors. The general features displayed by the panel of IgG polyreactive Abs include 1) skewed VH family usage with a predominance of VH1 and VH4 clones and a paucity of the normally prevalent VH3 family; 2) use of a variety of different VH germ-line genes within the context of the family usage and no restriction in D or JH gene usage; 3) skewed VL gene usage: 75% of Fabs used one of two germ lines; and 4) extensive somatic modification of both heavy and light chains. The importance of the heavy chain, in particular the heavy chain CDR3 (HCDR3), in dictating the polyreactive phenotype was demonstrated for the prototype Fab by chain shuffling and CDR transplantation experiments. in addition, and most strikingly, a constrained peptide based on the HCDR3 sequence was shown to be polyreactive and to inhibit binding of the parent Ab to a panel of Ags. A role for conformational flexibility in polyreactivity was suggested by a marked temperature dependence of Ab recognition of Ag. One Ab was shown to be polyreactive at 37 degrees C, but was apparently monoreactive at 4 degrees C. We hypothesize that Ab polyreactivity is associated with conformationally flexible HCDR3 regions in the context of certain favorable framework configurations.

Amino Acid Sequence↗
PubMed1996

Human neural tissues express a truncated Ror1 receptor tyrosine kinase, lacking both extracellular and transmembrane domains.

Human heart, lung and kidney express a 6 kb mRNA encoding Ror1, a member of the receptor tyrosine kinase (RTK) family with as yet unknown ligand specificity. We used a Ror1 cDNA probe to screen a cDNA library prepared from the human neuronogenic teratocarcinoma line, NTera2, and cloned a 2373 nucleotide transcript. This transcript contains an open reading frame that encodes a 388 amino acid protein identical with the cytosolic, C-terminal region of ror1 but lacking the ror1 transmembrane and entire extracellular domains. Northern blots demonstrate that mRNA encoding this truncated Ror1 ('t-Rorl') is abundantly expressed in fetal and adult human CNS, in human leukemia, lymphoma cell lines, and in a variety of human cancers derived from neuroectoderm. While previous studies have documented alternative splicing patterns within 5' and 3' regions of mRNAs encoding various RTKs altering their ligand binding specificity or their intracellular signaling, the present report is the first to demonstrate tissue-specific alternative mRNA splicing causing loss of the entire extracellular and transmembrane regions of an RTK.

Base Sequence↗
PubMed1997

Expression and characterization of recombinant porcine plasminogen activator inhibitor-1.

Porcine models are, among other animal models, very suitable for in vivo investigations in the vascular field especially with respect to the possible relationship between atherosclerosis and thrombosis. In order to use this model to define the in vivo role of PAI-1, the characterization of porcine PAI-1 and its availability for the generation of immunological tools are a prerequisite. Porcine plasminogen activator inhibitor-1 (poPAI-1) cDNA was isolated from a cDNA library prepared from cultured porcine aortic cells and characterized in comparison with PAI-1 cDNA's from other species including human, bovine, rabbit, rat and murine. Subsequently the DNA sequence coding the mature protein was cloned into an appropriate vector for expression in Escherichia coli and recombinant porcine PAI-1 was purified and characterized. On SDS-PAGE the apparent molecular weight was estimated to be 45 kDa, identical to the molecular weight of human PAI-1. The purified recombinant porcine PAI-1 (rpoPAI-1) had a specific activity of 508,800 +/- 800 U/mg (mean +/- SD, n = 3) towards human tissue-type plasminogen activator (ht-PA) and a functional half-life in vitro of 2.1 +/- 0.8 h (n = 3). Incubation with a two fold molar excess of ht-PA (n = 3) or human urokinase-type plasminogen activator (hu-PA, n = 2) followed by analysis by SDS-PAGE revealed reaction products corresponding to active (71 +/- 7% resp. 96 +/- 3.6%), latent (12 +/- 0.4% resp. 2.6 +/- 2.4%) and substrate (16.6 +/- 6.8% resp. 1.5 +/- 1.3) forms. Inactivated samples of porcine PAI-1 could be reactivated with guanidinium chloride up to 52% of its original specific activity towards t-PA and u-PA. The second order rate constant of inhibition of ht-PA was 1.64 +/- 0.37 10(7)M-1 s-1 (n = 9). In gel filtration rpoPAI-1 in buffer eluted at a volume corresponding to 24 kDa, whereas in the presence of porcine plasma, the molecular form containing PAI-1 activity eluted at a volume corresponding to 330 kDa, presumably as a consequence of binding of active PAI-1 to vitronectin. Taken together, these data demonstrate that no obvious functional differences exist between human and porcine PAI-1.

Amino Acid Sequence↗
PubMed1997

Expression of an anti-DNA-associated VH gene in immunized and autoimmune mice.

The J558 family BW-16 VH gene is closely associated with the autoimmune response to DNA of lupus-prone mice. We have followed the expression of VHBW-16-encoded heavy chains in cDNA libraries prepared from unmanipulated normal (C3H, AKR) and autoimmune (New Zealand Black/New Zealand White F1) mice, and from mice immunized with a highly immunogenic peptide/DNA complex. The prevalence, clonal heterogeneity, and structural properties (somatic mutation, complementarity-determining region 3 composition) of these H chains were investigated, and the DNA affinity of VHBW-16-encoded hybridoma mAb was measured in solution. We find that H chains encoded by VHBW-16 are very rare in Igs of normal mice, but increase significantly in peptide/DNA-immunized mice, and dramatically in diseased mice. The experimentally induced VHBW-16-encoded H chains are clonally restricted, somatically mutated, partly switched from IgM to IgG, and give rise to anti-DNA Abs with low affinity. In contrast, the VHBW-16-encoded H chains from diseased New Zealand Black/New Zealand White mice are clonally heterogeneous, exclusively of the IgG isotype, and produce high affinity anti-DNA autoantibodies. We conclude that the experimentally induced and spontaneous immune responses to DNA are qualitatively similar, but quantitatively different, and may truly reflect the principles of self immunologic tolerance.

Amino Acid Sequence↗
PubMed1997

Isolation and classification of a family of cyclin gene homologues in Lupinus luteus.

The lupine (Lupinus luteus cv. Ventus) cDNA clones encoding homologues of cyclin (CycB1;2, CycB1;3, CycB1;4) have been isolated from cDNA library prepared from roots inoculated with Bradyrhizobium lupini. Comparison of the deduced amino-acid sequences of CycB1;2, CycB1;3, CycB1;4 and previously described CycB1;1 (Deckert et al. 1996, Biochimie 78, 90-94) showed that they share 46-65% of identical amino acids. The presence of conserved residues (Renaudin et. al., in The Plant Cell Cycle, in the press; Renaudin et al., Plant Mol. Biol, in the press) along with phylogenetic analysis of known plant cyclins revealed that the four lupine sequences belong to subgroup 1 of B-like mitotic cyclins.

Amino Acid Sequence↗