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41.
Sequence variations in small-subunit ribosomal RNAs of Hartmannella vermiformis and their phylogenetic implications 总被引:1,自引:0,他引:1
Evidence of associations between free-living amoebas and human disease has
been increasing in recent years. Knowledge about phylogenetic relationships
that may be important for the understanding of pathogenicity in the genera
involved is very limited at present. Consequently, we have begun to study
these relationships and report here on the phylogeny of Hartmannella
vermiformis, a free-living amoeba that can harbor the etiologic agent of
Legionnaires' disease. Our analysis is based on studies of small-subunit
ribosomal RNA genes (srDNA). Nucleotide sequences were determined for
nuclear srDNA from three strains of H. vermiformis isolated from the United
Kingdom, Germany, and the United States. These sequences then were compared
with a sequence previously obtained for a North American isolate by J. H.
Gunderson and M. L. Sogin. The four genes are 1,840 bp long, with an
average GC content of 49.6%. Sequence differences among the strains range
are 0.38%-0.76%. Variation occurs at 19 positions and includes 2
single-base indels plus 14 monotypic and 3 ditypic single-base
substitutions. Variation is limited to eight helix/loop structures
according to a current model for srRNA secondary structure. Parsimony,
distance, and bootstrap analyses used to examine phylogenetic relationships
between the srDNA sequences of H. vermiformis and other eukaryotes
indicated that Hartmannella sequences were most closely related to those of
Acanthamoeba and the alga Cryptomonas. All ditypic sites were consistent
with a separation between European and North American strains of
Hartmannella, but results of other tests of this relationship were
statistically inconclusive.
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42.
Cell-to-cell transfer of glial proteins to the squid giant axon: The glia- neuron protein transfer hypothesis 下载免费PDF全文
The hypothesis that glial cells synthesize proteins which are transferred to adjacent neurons was evaluated in the giant fiber of the squid (Loligo pealei). When giant fibers are separated from their neuron cell bodies and incubated in the presence of radioactive amino acids, labeled proteins appear in the glial cells and axoplasm. Labeled axonal proteins were detected by three methods: extrusion of the axoplasm from the giant fiber, autoradiography, and perfusion of the giant fiber. This protein synthesis is completely inhibited by puromycin but is not affected by chloramphenicol. The following evidence indicates that the labeled axonal proteins are not synthesized within the axon itself. (a) The axon does not contain a significant amount of ribosomes or ribosomal RNA. (b) Isolated axoplasm did not incorporate [(3)H]leucine into proteins. (c) Injection of Rnase into the giant axon did not reduce the appearance of newly synthesized proteins in the axoplasm of the giant fiber. These findings, coupled with other evidence, have led us to conclude that the adaxonal glial cells synthesize a class of proteins which are transferred to the giant axon. Analysis of the kinetics of this phenomenon indicates that some proteins are transferred to the axon within minutes of their synthesis in the glial cells. One or more of the steps in the transfer process appear to involve Ca++, since replacement of extracellular Ca++ by either Mg++ or Co++ significantly reduces the appearance of labeled proteins in the axon. A substantial fraction of newly synthesized glial proteins, possibly as much as 40 percent, are transferred to the giant axon. These proteins are heterogeneous and range in size from 12,000 to greater than 200,000 daltons. Comparisons of the amount of amino acid incorporation in glia cells and neuron cell bodies raise the possibility that the adaxonal glial cells may provide an important source of axonal proteins which is supplemental to that provided by axonal transport from the cell body. These findings are discussed with reference to a possible trophic effect of glia on neurons and metabolic cooperation between adaxonal glia and the axon. 相似文献
43.
Ott CM Smith BD Portis AR Spreitzer RJ 《The Journal of biological chemistry》2000,275(34):26241-26244
In the active form of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC ), a carbamate at lysine 201 binds Mg(2+), which then interacts with the carboxylation transition state. Rubisco activase facilitates this spontaneous carbamylation/metal-binding process by removing phosphorylated inhibitors from the Rubisco active site. Activase from Solanaceae plants (e.g. tobacco) fails to activate Rubisco from non-Solanaceae plants (e.g. spinach and Chlamydomonas reinhardtii), and non-Solanaceae activase fails to activate Solanaceae Rubisco. Directed mutagenesis and chloroplast transformation previously showed that a proline 89 to arginine substitution on the surface of the large subunit of Chlamydomonas Rubisco switched its specificity from non-Solanaceae to Solanaceae activase activation. To define the size and function of this putative activase binding region, substitutions were created at positions flanking residue 89. As in the past, these substitutions changed the identities of Chlamydomonas residues to those of tobacco. Whereas an aspartate 86 to arginine substitution had little effect, aspartate 94 to lysine Rubisco was only partially activated by spinach activase but now fully activated by tobacco activase. In an attempt to eliminate the activase/Rubisco interaction, proline 89 was changed to alanine, which is not present in either non-Solanaceae or Solanaceae Rubisco. This substitution also caused reversal of activase specificity, indicating that amino acid identity alone does not determine the specificity of the interaction. 相似文献
44.
Pauline?AaltenEmail author Inez?HGB?Ramakers Geert?Jan?Biessels Peter?Paul?de Deyn Huiberdina?L?Koek Marcel?GM?OldeRikkert Ania?M?Oleksik Edo?Richard Lieke?L?Smits John?C?van Swieten Laura?K?Teune Aad?van der Lugt Frederik?Barkhof Charlotte?E?Teunissen Nico?Rozendaal Frans?RJ?Verhey Wiesje?M?van der Flier 《BMC neurology》2014,14(1):254
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49.
Forbidden synonymous substitutions in coding regions 总被引:2,自引:0,他引:2
In the evolution of highly conserved genes, a few "synonymous"
substitutions at third bases that would not alter the protein sequence are
forbidden or very rare, presumably as a result of functional requirements
of the gene or the messenger RNA. Another 10% or 20% of codons are
significantly less variable by synonymous substitution than are the
majority of codons. The changes that occur at the majority of third bases
are subject to codon usage restrictions. These usage restrictions control
sequence similarities between very distant genes. For example, 70% of third
bases are identical in calmodulin genes of man and trypanosome. Third-base
similarities of distant genes for conserved proteins are mathematically
predicted, on the basis of the G+C composition of third bases. These
observations indicate the need for reexamination of methods used to
calculate synonymous substitutions.
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50.
Human alpha-galactosidase A (alpha-Gal A) is the lysosomal glycohydrolase
that cleaves the terminal alpha-galactosyl moieties of various
glycoconjugates. Overexpression of the enzyme in Chinese hamster ovary
(CHO) cells results in high intracellular enzyme accumulation and the
selective secretion of active enzyme. Structural analysis of the N -linked
oligosaccharides of the intracellular and secreted glycoforms revealed that
the secreted enzyme's oligosaccharides were remarkably heterogeneous,
having high mannose (63%), complex (30%), and hybrid (5%) structures. The
major high mannose oligosaccharides were Man5-7GlcNAc2 species.
Approximately 40% of the high mannose and 30% of the hybrid
oligosaccharides had phosphate monoester groups. The complex
oligosaccharides were mono-, bi- , 2,4-tri-, 2,6-tri- and tetraantennary
with or without core-region fucose, many of which had incomplete outer
chains. Approximately 30% of the complex oligosaccharides were mono- or
disialylated. Sialic acids were mostly N -acetylneuraminic acid and
occurred exclusively in alpha2, 3-linkage. In contrast, the intracellular
enzyme had only small amounts of complex chains (7.7%) and had
predominantly high mannose oligosaccharides (92%), mostly Man5GlcNAc2 and
smaller species, of which only 3% were phosphorylated. The complex
oligosaccharides were fucosylated and had the same antennary structures as
the secreted enzyme. Although most had mature outer chains, none were
sialylated. Thus, the overexpression of human alpha-Gal A in CHO cells
resulted in different oligosaccharide structures on the secreted and
intracellular glycoforms, the highly heterogeneous secreted forms
presumably due to the high level expression and impaired glycosylation in
the trans- Golgi network, and the predominately Man5-7GlcNAc2 cellular
glycoforms resulting from carbohydrate trimming in the lysosome.
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