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At least 757 records · Page 42Linked to original sources
PubMed2001

Encoding of noxious stimulus intensity by putative pain modulating neurons in the rostral ventromedial medulla and by simultaneously recorded nociceptive neurons in the spinal dorsal horn of rats.

Neurons in the nucleus raphe magnus and adjacent structures of the rostral ventromedial medulla (RVM) are involved in the control of nociceptive transmission. In the RVM the so-called on-cells are excited, and the so-called off-cells are inhibited, by noxious stimuli applied almost anywhere on the body surface, thus showing that they receive information from spinal and trigeminal nociceptive neurons. In deeply anesthetized rats, recordings were made from RVM neurons that resembled on- and off-cells (herein called putative on- and off-cells) in order to investigate (1) how they encode the intensity of thermal noxious stimuli (46--56 degrees C) applied to a hindpaw, and (2) how their encoding properties relate to those of simultaneously recorded spinal neurons. In 49 of 98 cases, a graded increase in the stimulus temperature caused a monotonic decrease in the response latency of putative on-cells, putative off-cells and spinal neurons, while the response discharge rate monotonically increased for putative on-cells and spinal neurons and decreased for putative off-cells. In the majority of simultaneous recordings of RVM and spinal neurons, the latency and discharge rate of the putative on- or off-cell were highly correlated with the latency and discharge rate of the spinal neuron, and the stimulus/response slopes were similar. These results show that putative on- and off-cells can encode the stimulus intensity in terms of response latency and discharge rate, and suggest that such encoding closely reflects spinal neuronal encoding. This may be relevant for the transmission and modulation of pain information by RVM neurons.

Animals↗
PubMed2000

Cloning, characterization and chromosomal location of three genes encoding host-cell-wall-degrading enzymes in Leptosphaeria maculans, a fungal pathogen of Brassica spp.

The ascomycete, Leptosphaeria maculans, causes blackleg disease of oilseed Brassica spp. such as canola (Brassica napus). We have cloned a gene encoding endopolygalacturonase, pg1, and two genes encoding cellulases, cel1 and cel2, in L. maculans. These genes are not clustered in the genome, as they are located on different chromosomes. The deduced amino acid sequences of all three genes predict an N-terminal signal sequence, as is common for secreted fungal enzymes that degrade plant cell walls. The endopolygalacturonase encoded by pg1 shows the highest similarity (54% amino acid identity) to endopolygalacturonase 4 from Botrytis cinerea. Both cel1 and cel2 appear to encode cellobiohydrolase, and neither gene encodes a recognizable cellulose-binding domain or linker region. Transcription of pg1 is induced in cultures containing 1% polygalacturonic acid or pectin, and cel1 is induced in 1% cellulose or carboxymethylcellulose, as shown by Northern analysis. Glucose represses the induction of cel1 caused by cellulose and carboxymethylcellulose, but does affect transcription of pg1. Transcription of cel2 (but not cel1 or pg1) is detectable during infection of B. napus and B. juncea cotyledons and leaves using reverse transcription-PCR.

Amino Acid Sequence↗
PubMed1998

A conserved TN8TCCT motif in the octapeptide-encoding region of Pax genes which has the potential to direct cytosine methylation.

Our previous findings have shown that the developmental genes Pax7 and Pax3 are differentially methylated; the gene region that encodes the paired domain is hypomethylated, whereas the region that encodes the homeodomain is hypermethylated. For this reason, the known DNA sequence between the paired and homeoboxes was analysed for the presence of a conserved DNA motif to which a modifying protein could bind in order to direct the methylation or demethylation of surrounding gene sequences. The octapeptide-encoding region was found to contain several nucleotides that were highly conserved throughout the Pax gene family from phylogenetically distant species. The most conserved nucleotides are thought to comprise a motif TN8TCCT where N8=any combination of eight nucleotides. A conserved octapeptide-like-encoding sequence containing the TN8TCCT motif was also found in non-Pax genes of higher eukaryotes and in the non-coding strand of plants. Moreover, differential methylation seems to be associated with the presence of the TN8TCCT motif in p53 and the human oestrogen receptor genes. The presence of the TN8TCCT motif within an octapeptide-like-encoding sequence in human T-cell leukaemia virus type 1 might suggest that the putative recognition motif may have been introduced into various host genomes via some form of retroviral agent.

Amino Acid Sequence↗
PubMed2003

The centrosomal proteins pericentrin and kendrin are encoded by alternatively spliced products of one gene.

Pericentrin, a critical centrosome component first identified in mouse, recruits factors required for assembly of the mitotic spindle apparatus. A similar yet larger human protein named kendrin was recently identified, but its relationship to pericentrin was not clear. Extensive sequence homology between the mouse chromosome 10 region encoding pericentrin and the human chromosome 21 region encoding kendrin indicates that these proteins are encoded by syntenic loci. However, comparison of the published mouse pericentrin cDNA sequence to mouse genomic DNA sequences revealed two important differences: the stop codon present in the published mouse pericentrin cDNA is not found in the mouse genomic sequence, and the 3' end of the published mouse pericentrin cDNA is a fragment from a different mouse chromosome. To resolve these discrepancies, we sequenced a mouse expressed sequence tag (EST) that corresponds to the 3' end for a 7.1-kb mouse pericentrin RNA encoded on chromosome 10. Extensive northern blot analysis revealed that the pericentrin gene displays a complex expression pattern in both mouse and human: a 10-kb kendrin transcript is found in most tissues, whereas smaller transcripts are detected in a limited subset of tissues. These analyses demonstrate that pericentrin and kendrin are encoded by one gene, correct the previously published pericentrin cDNA sequence, and describe the complex expression pattern for a gene important for centrosome function in normal and transformed cells.

Alternative Splicing↗
PubMed2001

Effects of triazolam on brain activity during episodic memory encoding: a PET study.

It is well documented that acute administration of the benzodiazepine hypnotic drug triazolam (Halcion) impairs episodic memory encoding. We examined the neuroanatomical substrates of this effect in healthy adult volunteers using a double-blind, within-subject design. Following oral capsule administration (0.25 mg/70 kg triazolam or placebo), regional cerebral blood flow (rCBF) was measured using positron emission tomography (PET) with 15O-H(2)O during the performance of semantic categorization, orthographic categorization, and visual fixation (resting) tasks. rCBF associated with episodic memory encoding was measured by the difference in rCBF during the orthographic categorization task relative to that during the semantic categorization task. Results in the placebo condition (n = 9) replicated those of previous nonpharmacological encoding studies (activation in the left prefrontal cortex, cerebellum, anterior cingulate cortex, temporal cortex, and occipital cortex). Relative to placebo, results in the triazolam condition (n = 6) revealed significantly impaired memory performance, and deactivation during encoding in a subset of areas shown previously to be associated with encoding (anterior cingulate cortex, cerebellum, and precuneus). Results are discussed in relation to triazolam's effects on mnemonic versus attentional processes.

Adult↗
PubMed2003

Encoding of vibrissal active touch.

Mammals acquire much of their sensory information by actively moving their sensory organs. Yet, the principles of encoding by active sensing are not known. Here we investigated the encoding principles of active touch by rat whiskers (vibrissae). We induced artificial whisking in anesthetized rats and recorded from first-order neurons in the trigeminal ganglion. During active touch, first-order trigeminal neurons presented a rich repertoire of responses, which could not be inferred from their responses to passive deflection stimuli. Individual neurons encoded four specific events: whisking, contact with object, pressure against object, and detachment from object. Whisking-responsive neurons fired at specific deflection angles, reporting the actual whiskers' position with high precision. Touch-responsive neurons encoded the horizontal coordinate of objects' position by spike timing. These findings suggest two specific encoding-decoding schemes for horizontal object position in the vibrissal system.

Action Potentials↗
PubMed2001

Electrophysiological correlates of memory encoding are task-dependent.

Event-related potentials (ERPs) were used to investigate whether the neural correlates of successful episodic encoding differ according to the nature of the study task. At study, 16 subjects were cued to make either animacy or alphabetic decisions about visually presented words. A recognition memory test with confidence judgements followed after a delay of 30 min. For the animacy task, words that were subsequently confidently recognised were associated with a positive-going ERP modulation. By contrast, for the alphabetic task, confident recognition was associated with a negative-going ERP modulation. Both types of subsequent memory effects started shortly after word onset. These findings suggest that the neural correlates of memory encoding differ qualitatively, rather than quantitatively, according to the nature of the study task. Episodic encoding thus seems to be supported by multiple, task-specific, neural systems. The early onset of these memory effects suggests that episodic encoding can be facilitated by processes that start before the onset of the to-be-encoded item.

Adolescent↗
PubMed1999

Frontotemporal interactions in face encoding and recognition.

Cognition may result from different patterns of neural interactions distributed across the brain. If this is true then across different cognitive tasks different functional interactions should be observed within an anatomical network. To investigate this hypothesis, a network analysis of PET data obtained from a face memory study was conducted. PET scans were obtained while subjects performed face perception, face encoding and face recognition tasks. Partial least squares (PLS) analysis of rCBF was used to identify brain regions that were engaged during these tasks, and anatomically based structural equation modeling (SEM) was used to construct functional models for matching, encoding and recognition. There was some overlap in the functional interactions observed across the three cognitive tasks. In all three tasks, there were positive interactions involving the left occipitotemporal regions. These interactions may represent the perceptual component of the three tasks. Task-specific functional interactions were also observed. During face encoding, there was a bilateral positive influence of occipitotemporal regions on medial temporal regions. In addition, there were positive interhemispheric interactions between middle temporal regions and between limbic regions during encoding. These patterns may reflect the participation of medial temporal cortex in the formation of new memories. In the face recognition task, there was a positive loop in the right hemisphere from occipital cortex to frontal cortex and back from frontal cortex to occipitotemporal cortex. In addition, there was a strong positive input into the right hippocampal region from right occipitotemporal cortex. This pattern of interaction was specific to the recognition task and might represent the process whereby the input faces are compared to the internal representation laid down during encoding, thus enabling recognition.

Adult↗
PubMed2001

Novel small RNA-encoding genes in the intergenic regions of Escherichia coli.

BACKGROUND: Small, untranslated RNA molecules were identified initially in bacteria, but examples can be found in all kingdoms of life. These RNAs carry out diverse functions, and many of them are regulators of gene expression. Genes encoding small, untranslated RNAs are difficult to detect experimentally or to predict by traditional sequence analysis approaches. Thus, in spite of the rising recognition that such RNAs may play key roles in bacterial physiology, many of the small RNAs known to date were discovered fortuitously. RESULTS: To search the Escherichia coli genome sequence for genes encoding small RNAs, we developed a computational strategy employing transcription signals and genomic features of the known small RNA-encoding genes. The search, for which we used rather restrictive criteria, has led to the prediction of 24 putative sRNA-encoding genes, of which 23 were tested experimentally. Here we report on the discovery of 14 genes encoding novel small RNAs in E. coli and their expression patterns under a variety of physiological conditions. Most of the newly discovered RNAs are abundant. Interestingly, the expression level of a significant number of these RNAs increases upon entry into stationary phase. CONCLUSIONS: Based on our results, we conclude that small RNAs are much more widespread than previously imagined and that these versatile molecules may play important roles in the fine-tuning of cell responses to changing environments.

Blotting, Northern↗
PubMed1996

Isotope or mass encoding of combinatorial libraries.

BACKGROUND: Combinatorial chemistry using solid-phase synthesis is a rapidly developing technology that can result in a significant reduction in the time required to find and optimize lead compounds. The application of this approach to traditional medicinal chemistry has led to the construction of libraries of small organic molecules on resin beads. A major difficulty in developing large combinatorial libraries is the lack of a facile encoding and decoding methodology to identify active compounds. RESULTS: Several encoding schemes are described which use the ability of mass spectrometry to ascertain isotopic distributions. Molecular tags are attached to resin beads in parallel or on the linker used for chemical library synthesis. The tags are encoded via a controlled ratio of a number of stable isotopes on the tagging molecules, and range from a single to a complex isotopic distribution. CONCLUSIONS: A novel coding scheme is described that is useful for the generation of large encoded combinatorial libraries. The code can be cleaved after assay and analyzed by mass spectrometry in an automated fashion. An important element of the combinatorial discovery process is the ability to extract the structure-activity relationship (SAR) information made available by library screening. The speed and sensitivity of the mass-encoding scheme has the potential to determine the full SAR for a given library.

Chemistry, Organic↗
PubMed2000

Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae.

The product of the LPP1 gene in Saccharomyces cerevisiae is a membrane-associated enzyme that catalyzes the Mg(2+)-independent dephosphorylation of phosphatidate (PA), diacylglycerol pyrophosphate (DGPP), and lysophosphatidate (LPA). The LPP1-encoded lipid phosphatase was overexpressed 681-fold in Sf-9 insect cells and used to examine the enzymological properties of the enzyme using PA, DGPP, and LPA as substrates. The optimum pH values for PA phosphatase, DGPP phosphatase, and LPA phosphatase activities were 7. 5, 7.0, and 7.0, respectively. Divalent cations (Mn(2+), Co(2+), and Ca(2+)), NaF, heavy metals, propranolol, phenylglyoxal, and N-ethylmaleimide inhibited the PA phosphatase, DGPP phosphatase, and LPA phosphatase activities of the enzyme. The inhibitory effects of N-ethylmaleimide and phenylglyoxal on the LPP1-encoded enzyme were novel properties when compared with other Mg(2+)-independent lipid phosphate phosphatases from S. cerevisiae and mammalian cells. The LPP1-encoded enzyme exhibited saturation kinetics with respect to the surface concentrations of PA (K(m)=0.05 mol%), DGPP (K(m)=0.07 mol%), and LPA (K(m)=0.08 mol%). Based on specificity constants (V(max)/K(m)LPA (1.3 units/mg/mol%). DGPP (K(i)=0.12 mol%) was a competitive inhibitor with respect to PA, and PA (K(i)=0.12 mol%) was a competitive inhibitor with respect to DGPP. This suggested that the binding sites for these substrates were the same. The enzymological properties of the LPP1-encoded enzyme differed significantly from those of the S. cerevisiae DPP1-encoded lipid phosphatase, a related enzyme that also utilizes PA, DGPP, and LPA as substrates.

Animals↗
PubMed2001

Characterization of three genes encoding enzymes of the folate biosynthetic pathway in Plasmodium falciparum.

Although the folate metabolic pathway in malaria parasites is a major chemotherapeutic target, resistance to currently available antifolate drugs is an increasing problem. This pathway, however, includes a number of enzymes that, to date, have not been characterized despite their potential for clinical exploitation. As a step towards evaluation of additional targets in this pathway, we report the isolation and characterization of 3 new genes that encode homologues of GTP cyclohydrolase I (GTP-CH), dihydrofolate synthase/folylpolyglutamate synthase (DHFS/FPGS) and serine hydroxymethyltransferase (SHMT). The genes encoding GTP-CH and SHMT are unambiguously assigned to chromosome 12, while that for DHFS/FPGS is tentatively assigned to chromosome 13. All 3 genes are expressed in blood-stage parasites, yielding transcripts of which only ca 60-70% is accounted for by coding sequence. All 3 of the proteins predicted to be encoded by these genes display sequence differences compared to the human host homologues that may be of functional significance. These data bring the complement of cloned genes that encode activities in the pathway to seven, leaving only the gene encoding dihydroneopterin aldolase (DHNA) to be identified in the route from GTP to folate synthesis and folate turnover in the thymidylate cycle.

Aldehyde-Lyases↗
PubMed1987

Use of consensus oligonucleotides for detecting and isolating nucleic acids encoding calcium binding domains of the troponin C superfamily.

Proteins belonging to the troponin C superfamily (troponin C, calmodulin, myosin light chains, and parvalbumin) are involved in a wide variety of cellular activities mediated by calcium ions. Most of these proteins bind ionic calcium, and all have calcium binding domains that are conserved to some extent at the nucleic acid level. We made use of the conservation in the third calcium binding domain to synthesize two consensus sequence oligonucleotide probes, one 43 bases and the other 25 bases long. By using cDNA and genomic clones encoding calmodulin, troponin C, parvalbumin, and the sea urchin Spec proteins, we show that these probes hybridize with nucleic acid sequences representing calcium binding domains. In an RNA gel blot analysis of embryonic RNA from the sea urchin Strongylocentrotus purpuratus, we show that transcripts which have previously been shown to encode troponin C like proteins hybridize with the consensus sequence probes. Screening sea urchin cDNA and genomic libraries with the 43-base consensus oligonucleotide shows that the probe can be used to isolate cloned nucleic acids. Two such genomic clones from a Lytechinus pictus library were isolated and characterized. One clone encodes part of an L. pictus calmodulin gene, and the other encodes a member of the superfamily that has not been characterized previously. The consensus oligonucleotides should be valuable probes in the diagnosis and isolation of nucleic acids encoding proteins of the troponin C superfamily.

Amino Acid Sequence↗
PubMed2004

Only one of the two annotated Lactococcus lactis fabG genes encodes a functional beta-ketoacyl-acyl carrier protein reductase.

The small genome of the Gram-positive bacterium Lactococcus lactis ssp. lactis IL1403 contains two genes that encode proteins annotated as homologues of Escherichia coli beta-hydroxyacyl-acyl carrier protein (ACP) reductase. E. coli fabG encodes beta-ketoacyl-acyl carrier protein (ACP) reductase, the enzyme responsible for the first reductive step of the fatty acid synthetic cycle. Both of the L. lactis genes are adjacent to (and predicted to be cotranscribed with) other genes that encode proteins having homology to known fatty acid synthetic enzymes. Such relationships have often been used to strengthen annotations based on sequence alignments. Annotation in the case of beta-ketoacyl-ACP reductase is particularly problematic because the protein is a member of a vast protein family, the short-chain alcohol dehydrogenase/reductase (SDR) family. The recent isolation of an E. coli fabG mutant strain encoding a conditionally active beta-ketoacyl-ACP reductase allowed physiological and biochemical testing of the putative L. lactishomologues. We report that expression of only one of the two L. lactis proteins (that annotated as FabG1) allows growth of the E. coli fabG strain under nonpermissive conditions and restores in vitro fatty acid synthetic ability to extracts of the mutant strain. Therefore, like E. coli, L. lactis has a single beta-ketoacyl-ACP reductase active with substrates of all fatty acid chain lengths. The second protein (annotated as FabG2), although inactive in fatty acid synthesis both in vivo and in vitro, was highly active in reduction of the model substrate, beta-ketobutyryl-CoA. As expected from work on the E. coli enzyme, the FabG1 beta-ketobutyryl-CoA reductase activity was inhibited by ACP (which blocks access to the active site) whereas the activity of FabG2 was unaffected by the presence of ACP. These results seem to be an example of a gene duplication event followed by divergence of one copy of the gene to encode a protein having a new function.

Alcohol Oxidoreductases↗
PubMed2004

Encoding method for OBOC small molecule libraries using a biphasic approach for ladder-synthesis of coding tags.

In the "one-bead one-compound" (OBOC) combinatorial library method, each compound bead displays only one compound entity. Hundreds of thousands to millions of compound beads can be synthesized rapidly and screened simultaneously. Positive compound beads are then isolated for structural analysis. To fully exploit the power of OBOC combinatorial small molecule libraries, a robust and high throughput encoding method is needed to decode the positive compound beads. In this paper, we report on the development of a novel encoding strategy that combines the concepts of ladder-synthesis and chemical encoding on bilayer beads. In these encoded libraries, small molecule compounds are displayed on the bead surface, and cleavable coding tags consisting of a series of truncated molecules reside in the bead interior. Such a library can be easily constructed using the biphasic approach (J. Am. Chem. Soc.2002, 124, 7678) to topologically segregate the functionalities of the beads during library synthesis. The ladder members and coding tags are then released for MALDI-TOF-MS analysis. To simplify the interpretation of the mass spectra, we purposely add bromine into the cleavable linker so that the cleavage products generate a characteristic isotope fingerprint. The chemical structure of library compounds can be determined by analyzing the mass differences between adjacent peaks on the mass spectra. This encoding strategy also provides valuable information on the quality of the testing compound on the surface of the bead. To validate this methodology, a model OBOC small molecule library with 12,288 members was synthesized on TentaGel beads and screened against streptavidin. The chemical structures of the compound on each positive bead were unambiguously identified.

Amino Acids↗
PubMed1999

Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae.

The red algal chloroplast genome encodes an essential prokaryotic cell division gene, ftsH, which has never been found in the mitochondrial genome of any organism. To compare the conserved prokaryote-derived mechanism for mitochondrial division with that of chloroplasts, we cloned chloroplast- and nuclear-encoded ftsH genes from the primitive red alga Cyanidioschyzon merolae. The deduced amino-acid sequence of chloroplast ftsH (ftsHcp) consists of 603 amino acids and shows the highest similarity with algal-chloroplast and cyanobacterial FtsH. On the other hand, the nuclear-encoded ftsH (ftsH2) encodes a protein of 920 amino acids and has the highest similarity with two yeast mitochondrial FtsHs, Rca1p and Afg3p. Furthermore, the amino-terminal extension of FtsH2 appears to be an amphipathic alpha-helix, a characteristic mitochondrial targeting signal, suggesting that FtsH2 is a mitochondrial protein. Southern hybridization revealed that ftsH2 is a single gene located on chromosome III of the 17 C. merolae chromosomes. The level of expression of the 3.0 and 4.0 kb transcripts of this gene decreased in concert during the organelle division phase of a synchronized culture, indicating a cell-cycle-dependent manner of ftsH2 transcription, while northern hybridization did not detect ftsHcp transcripts. Nevertheless, reverse transcription-PCR and immunoblotting demonstrated for the first time that chloroplast-encoded ftsH is transcriptionally and translationally active. Overproduction of FtsHcp and FtsH2 in Escherichia coli disrupted cytokinesis and produced filamentous cells, but had no effect on the replication, segregation, or distribution of their nucleoids, as also occurs in ftsH-deficient E. coli. These observations suggest the possible involvement of both C. merolae FtsHs in organelle division.

ATP-Dependent Proteases↗
PubMed1999

Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol dehydrogenase enzyme in lucerne (Medicago sativa L.)

A lucerne (alfalfa, Medicago sativa) stem cDNA library was screened with a cinnamyl-alcohol dehydrogenase (CAD) cDNA probe from tobacco (Nicotiana tabacum cv. Samsun). Two distinctly different cDNA clones (54% identical) were isolated and identified as putative CAD-encoding cDNAs by comparison of their nucleotide sequences with those of CAD-encoding DNA sequences from other plant species. One of the cDNAs, MsaCad2, was found to be 99.4% identical at the nucleotide level to the previously isolated lucerne cad cDNA which encodes a CAD isoform involved in lignin biosynthesis. The other cDNA, MsaCad1, has not been reported previously in lucerne, and encodes a protein related to the ELI3 class of elicitor-inducible defence-related plant proteins. The MsaCad1- and MsaCad2-encoded proteins were expressed in Escherichia coli and CAD1 was shown to be active with a range of cinnamyl, benzyl and aliphatic aldehyde substrates, while CAD2 was specific for the cinnamyl aldehydes only. Each of the respective genes is present as one or two copies. The MsaCad1 gene is expressed most actively in stem and floral tissue, whereas MsaCad2 is most actively expressed in stem, hypocotyl and root tissue. In stem tissue, expression of both genes occurs predominantly in internodes 4 and 5 (from the apex). MsaCad2, in contrast to MsaCad1, is not significantly expressed in the top three internodes of the stem. Both MsaCad1 and MsaCad2 are wound-inducible, and the wound-responsiveness of each gene is modulated by salicylic acid.

Alcohol Oxidoreductases↗
PubMed1999

Selection of Arabidopsis genes encoding secreted and plasma membrane proteins.

Secreted and plasma membrane proteins play crucial roles in a variety of physiological and developmental processes of multicellular organisms. Systematic cloning of the genes encoding these proteins is therefore of general interest. An effective method of trapping signal sequences was first described by Tashiro et al. (1993), and a similar yet more efficient method was reported by Klein et al. (1996) and Jacobs et al. (1997). In this study, we carried out the latter yeast-based signal sequence trap to clone genes from Arabidopsis thaliana encoding secreted and plasma membrane proteins. Of 144 sequenced cDNA clones, 18% are identical to previously cloned Arabidopsis thaliana genes, 12% are homologous to genes identified from various organisms, and 46% are novel. All of the isolated genes identical or homologous to previously reported genes are either secreted or plasma membrane proteins, and the remaining novel genes appear to contain functional signal sequences based on computer-aided sequence analysis. The full-length cDNA clones of one homologous gene and another novel gene were isolated and sequenced. The deduced amino acid sequences suggest that the former encodes a secreted protein, and the latter encodes a type 1 membrane protein. These results indicate that the signal sequence trap method is effective and useful for the isolation of plant genes encoding secreted and plasma membrane proteins.

Amino Acid Sequence↗