Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We present here a 1770 bp-long cDNA which encodes a murine type II keratin. Sequence comparisons of the keratin with those of various type II keratins expressed in mouse epidermis and internal stratified epithelia reveal that the new keratin is unrelated to epithelial keratins. Rather the structural organization of its amino- and carboxyterminal domains and the high content of cysteine and proline residues in these regions suggest that the keratin represents a murine type II hair keratin. This assumption was confirmed by in situ hybridization which localized the mRNA of the keratin in upper cells of the hair cortex and in suprabasal cells of the central core unit of filiform papillae of the tongue. Hybrid selection analyses revealed that the keratin has a molecular weight of 58 kD. It remains to be seen whether the keratin corresponds to MHb 3 or MHb 4.
Mol Biol Rep 1992 Feb
PMID:Structure and site of expression of a murine type II hair keratin. 137 89

The maxicircle of Trypanosoma brucei encodes components of the mitochondrial oxidative phosphorylation system, as do other mitochondrial DNAs, but maxicircle gene identification is complicated by extensive editing of some transcripts. We found that transcripts from the CR1 region were extensively edited, as are other transcripts from maxicircle regions which exhibit strong G versus C strand bias. Editing added 259 uridines and removed 46 uridines to produce an approximately 574-nucleotide mature mRNA. Partially edited cDNAs and potential guide RNAs were also characterized. Initiation and termination codons were created, and they defined an open reading frame encoding a predicted protein of 145 amino acids. This protein contains two iron-sulfur cysteine motifs and is homologous to a subunit of NADH dehydrogenase and to other electron-carrier proteins. Higher levels of both edited and unedited CR1 transcripts accumulated in bloodstream forms of the parasite than in procyclic forms, suggesting developmental regulation of CR1 gene expression.
Mol Cell Biol 1992 May
PMID:Maxicircle CR1 transcripts of Trypanosoma brucei are edited and developmentally regulated and encode a putative iron-sulfur protein homologous to an NADH dehydrogenase subunit. 137 7

We have isolated an ovine insulin-like growth factor-binding protein-2 (IGFBP-2) cDNA from an adult sheep cDNA library, to determine the structure of ovine IGFBP-2 and to examine the pattern of IGFBP-2 gene expression in adult sheep tissues. This cDNA had 81, 96 and 87% identity with the rat, bovine and human sequences respectively. The deduced amino acid sequence of the ovine IGFBP-2 showed 86, 95 and 85% homology with the rat, bovine and human peptide sequences respectively. The ovine IGFBP-2 cDNA encoded a precursor protein of 317 amino acids which comprised a 33 residue hydrophobic leader sequence and a 284 residue, 30.9 kDa, mature peptide. The 18 cysteine residues, which are a characteristic feature of IGFBPs, were conserved. Also, an Arg-Gly-Asp (RGD) sequence near the C terminus was present. A single transcript of approximately 1.5 kb was expressed in abundance in selected tissues of an adult sheep, namely liver, kidney, adrenal, pituitary and choroid plexus. Southern blot analysis of ovine genomic DNA with the cDNA probe demonstrated that IGFBP-2 is encoded by a single gene. These findings indicate that the ovine IGFBP-2 protein is similar to that in other species and that, in the adult, the mRNA is expressed only in selected tissues.
J Mol Endocrinol 1992 Aug
PMID:The characterization and expression of ovine insulin-like growth factor-binding protein-2. 138 Nov 82

A chitinase cDNA clone from rapeseed (Brassica napus L. ssp. oleifera) was isolated. The cDNA clone, ChB4, represents a previously purified and characterized basic chitinase isozyme. The longest open reading frame in ChB4 encodes a polypeptide of 268 amino acids. This polypeptide consists of a 24 amino acid N-terminal signal peptide, a cysteine-rich domain and a catalytic domain. The primary structure of the mature ChB4 shows a low degree of identity with class I and II chitinases, 43-48% and 35%, respectively. In contrast, ChB4 shows 62% identity to a basic sugar-beet chitinase and 63% identity to an acidic chitinase from bean. The expression of chitinase messenger RNA (mRNA) in response to infection with Phoma lingam (Tode ex. Fr.) Desm. was examined by northern hybridization and scintilation counting. A differential induction was seen between resistant and susceptible cultivars where 3-fold higher chitinase transcript levels were estimated one day after inoculation in resistant as compared to susceptible cultivar. This difference diminished eight days after inoculation. Southern hybridization analysis indicates that the chitinase is encoded by a small family of genes.
Plant Mol Biol 1992 Oct
PMID:Cloning and characterization of a pathogen-induced chitinase in Brassica napus. 139 71

The complete amino acid sequence of acidic chitinase from yam (Dioscorea japonica) aerial tubers was determined. The protein is composed of a single polypeptide chain of 250 amino acid residues and has a calculated molecular mass of 27,890 Da. There is an NH2-terminal domain, a hinge region, and a main structure, typical for class I chitinases (Shinshi, H., Neuhaus, J.-M., Ryals, J., and Meins, F., Jr. (1990) Plant Mol. Biol. 14, 357-368). We have obtained the first evidence for an acidic class I chitinase. Comparison with sequences of other class I chitinases revealed approximately 40% sequence similarity, a value lower than that for other class I chitinases (70-80%). We assume that there is a local conformational change in the molecule; cysteine residues that probably form disulfide bonds are completely conserved, with the exception of Cys-178. The difference in structure between this chitinase and other basic class I chitinases suggests that acidic and basic isoforms should be grouped into subclasses; this protein is an ethylene- or a pathogen-independent chitinase produced by a gene that is inherent in the tuber.
 ...
PMID:The complete amino acid sequence of yam (Dioscorea japonica) chitinase. A newly identified acidic class I chitinase. 140 Mar 11

The gene encoding the streptococcal flavoprotein NADH oxidase (NOXase), which catalyzes the four-electron reduction of O2-->2H2O, has been cloned and sequenced from the genome of Streptococcus (Enterococcus) faecalis 10C1 (ATCC 11700). The deduced NOXase protein sequence corresponds to a molecular mass of 48.9 kDa and contains three previously sequenced cysteinyl peptides obtained with the purified enzyme. In Escherichia coli, the expressed nox gene produced a catalytically active product, which retained its immunoreactivity to affinity-purified NOXase antisera. Alignment of the NOXase protein sequence with that of streptococcal NADH peroxidase (NPXase) revealed that the proteins are 44% identical. Among the most highly conserved segments is a sequence containing Cys42; this residue is known to exist as a stabilized cysteine-sulfenic acid (Cys-SOH) in NPXase and serves as the non-flavin redox center. In addition, three previously identified NPXase segments, known to be involved in FAD and NAD(P)-binding in other pyridine nucleotide-linked flavoprotein oxidoreductases, are strongly conserved in NOXase. Overall, the extensive homology observed between NOXase and NPXase suggests that the monomer chain fold of the oxidase closely resembles that of the peroxidase. Both sequences share limited but significant homology to those of glutathione reductase and other members of the flavoprotein disulfide reductase family. These and other considerations suggest that these two unusual streptococcal flavoproteins constitute a distinct class of FAD-dependent oxidoreductases, the flavoprotein peroxide reductases, easily contrasted with enzymes such as glutathione reductase and thioredoxin reductase.
J Mol Biol 1992 Oct 05
PMID:Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases. 140 82

The three-dimensional structure of telokin, an acidic protein identical to the C-terminal portion of smooth muscle myosin light chain kinase from turkey gizzard, has been determined at 2.8 A resolution and refined to a crystallographic R-factor of 19.5% for all measured X-ray data from 30 A to 2.8 A. Crystals used in the investigation belonged to the space group P3(2)21, with one molecule per asymmetric unit and unit cell dimensions of a = b = 64.4 A and c = 50.6 A. Telokin contains 154 amino acid residues, 103 of which were visible in the electron density map. The overall molecular fold of telokin consists of seven strands of antiparallel beta-pleated sheet that wrap around to form a barrel. There is also an extended tail of eight amino acid residues at the N terminus that does not participate in beta-sheet formation. The beta-barrel can be simply envisioned as two layers of beta-sheet, nearly parallel to one another, with one layer containing four and the other three beta-strands. This type of beta-barrel, as seen in telokin, was first observed for the CH2 domain of an immunoglobulin fragment Fc. Telokin is an intracellular protein and, as such, does not contain the disulphide linkage between beta-strands B and F normally observed in the immunoglobulin constant domains. It does, however, contain two cysteine amino acid residues (Cys63 and Cys115) that are situated at structurally identical positions to those forming the disulphide linkage in the immunoglobulin constant domain.
J Mol Biol 1992 Oct 05
PMID:X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. 140 91

Arginine auxotrophs of the dinitrogen-fixing cyanobacterium Anabaena species strain PCC 7120 were isolated after ultraviolet light mutagenesis and penicillin enrichment. Two of these auxotrophs were complemented by a cosmid gene library of the wild-type strain established in Escherichia coli that was transferred en masse to the mutants by conjugation. The gene complementing one of those mutants was found to complement an E. coli argC mutant. Sequencing analysis of the gene showed that it encodes a 322-residue polypeptide that is homologous to the ArgC protein of E. coli, Bacillus subtilis and Streptomyces clavuligerus and to the C-terminal moiety of the Saccharomyces cerevisiae ARG5,6 gene product, N-acetylglutamate semialdehyde dehydrogenase. A cysteine residue present in a highly conserved domain in the five proteins is probably located in the active site of the enzyme. Conserved among the ArgC proteins, sequences resembling the primary structure of nucleotide-binding domains are also found. Downstream of the Anabaena argC gene seven nearly perfect repeats of a heptanucleotide (consensus sequence:5'-CTAATGA-3') are found.
Mol Microbiol 1992 Aug
PMID:Isolation of arginine auxotrophs, cloning by mutant complementation, and sequence analysis of the argC gene from the cyanobacterium Anabaena species PCC 7120. 140 50

We report the construction and the expression in Escherichia coli of three different fusion genes encoding the extended human IgG3 hinge region (Hi) fused in-phase to the C-terminal end of bacterial TEM1 beta-lactamase (Bla). In the first fusion gene blahi, TEM1 beta-lactamase (Bla). In the first fusion gene blahi, the hinge sequence was directly coupled to the 3' end of the beta-lactamase gene, whereas in the two other constructs, blal1hi and blal2hi, a linker encoding 14 and 10 amino acids, respectively, was inserted between the two subunits. After expression (24 h, 20 degrees C) under control of the constitutive kanamycin phosphoribosyl transferase promoter, the fusion proteins, BlaHi, BlaL1Hi and BlaL2Hi, respectively, were almost exclusively detected in the periplasmic fraction, and they conferred carbenicillin-resistance to the cells. These results indicate that beta-lactamase can efficiently direct the export of proteins fused to its C-terminus, and moreover, at least some of the exported fusion proteins must carry the beta-lactamase moiety in a properly folded form. Analysis of their assembly, however, revealed that only a minor fraction was recovered as the expected F(ab')2-like dimer. The presence in the periplasm of 'oxidized' monomers (with intrachain disulphide bonds) as well as of several high-molecular-mass proteins, probably resulting from the association between monomers and other cysteine-rich proteins, strongly suggests that the conditions in the bacterial periplasm are insufficient to allow proper assembly of multimeric proteins with several interchain disulphide bonds.
Mol Microbiol 1992 Aug
PMID:Disulphide bridge formation in the periplasm of Escherichia coli: beta-lactamase:: human IgG3 hinge fusions as a model system. 140 60

Southern blotting of bovine genomic DNA and hybridization with a human Fc gamma RI cDNA probe, p135, has identified a single copy of the bovine Fc gamma RI gene. A bovine genomic lymphocyte library in lambda EMBL3 was screened with probe p135. A positive lambda clone, 15.5.4, containing the three extracellular domain exons of Fc gamma RI, has been cloned, mapped and sequenced. Each extracellular domain is encoded within a single exon. All three domains are assigned to the C-2 set of the Ig superfamily with 58% identity between amino acid residues of bovine, human and mouse Fc gamma RI. Pairs of cysteine residues are conserved in each domain as potential sites for intra-chain disulphide bonding. Human monocytoid U937 cells were used as a model to test binding homology within the Fc gamma RI family. The binding of IgG isotypes to IFN-gamma stimulated U937 cells was determined by FACScan flow cytometry. U937 cell Fc gamma RI receptor does not bind bovine or ovine IgG isotypes. On the basis of these studies and by comparison of the Fc determinant region sequences of IgG, the introduction of species specificity in Fc gamma RI/IgG interaction by evolutionary drift is proposed.
Mol Immunol 1992 Nov
PMID:Genomic organisation and sequence of the extracellular domain exons of the bovine Fc gamma RI receptor, and evidence for restricted binding of ruminant IgG to U937 cells. 140 25


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>