Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The polypeptide composition of the Photosystem I complex from Synechococcus sp. PCC 6301 was determined by sodium-dodecyl sulfate polyacrylamide gel electrophoresis and N-terminal amino acid sequencing. The PsaA, PsaB, PsaC, PsaD, PsaE, PsaF, PsaK and PsaL proteins, as well as three polypeptides with apparent masses less than 8 kDa and small amounts of the 12.6 kDa GlnB (PII) protein, wee present in the Photosystem I complex. No proteins homologous to the PsaG and PsaH subunits of eukaryotic Photosystem I complexes were detected. When the Photosystem I complex was treated with 6.8 M urea and ultrafiltered using a 100 kDa cutoff membrane, the resulting Photosystem I core protein was found to be depleted of the PsaC, PsaD and PsaE proteins. The filtrate contained the missing proteins, along with five proteolytically-cleaved polypeptides with apparent masses of less than 16 kDa and with N-termini identical to that of the PsaD protein. The PsaF and PsaL proteins, along with the three less than 8 kDa polypeptides, were not released from the Photosystem I complex to any significant extent, but low-abundance polypeptides with N-termini identical to those of PsaF and PsaL were found in the filtrate with apparent masses slightly smaller than those found in the native Photosystem I complex. When the filtrate was incubated with FeCl3, Na2S and beta-mercaptoethanol in the presence of the isolated Photosystem I core protein, the PsaC, PsaD and PsaE proteins were rebound to reconstitute a Photosystem I complex functional in light-induced electron flow from P700 to FA/FB. In the absence of the iron-sulfur reconstitution agents, there was little rebinding of the PsaC, psaD or PsaE proteins to the Photosystem I core protein. No binding of the truncated PsaD polypeptides occurred, either in the presence or absence of the iron-sulfur reagents. The reconstitution of the FA/FB iron-sulfur clusters thus appears to be a necessary precondition for rebinding of the PsaC, psaD and psaE proteins to the Photosystem I core protein.
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PMID:Polypeptide composition of the Photosystem I complex and the Photosystem I core protein from Synechococcus sp. PCC 6301. 165 17

Five mouse hybridomas which produce monoclonal antibodies against the p17 core protein of HIV-1 have been isolated. Cross-competition assays and mapping with synthetic peptides demonstrate that two closely related epitopes are identified by these antibodies. Directed against two neighbouring peptides at the carboxy-terminal end of the molecule, they can be used for the selective detection of p17 polypeptide in a viral extract or in an infected cell lysate by a solid-phase sandwich enzyme immunoassay.
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PMID:Characterization of monoclonal antibodies against the p17 core protein of the human immunodeficiency virus 1. 169 Dec 36

Bovine corneal keratan sulfate proteoglycan (KSPG) contains two core proteins, 37 and 25 kDa, if fully deglycosylated, but 47 and 35 kDa, respectively, after endo-beta-galactosidase (Funderburgh, J. L., and Conrad, G. W. (1990) J. Biol Chem. 265, 8297-8303). Chicken corneal KSPG released a single core protein of 47 kDa after endo-beta-galactosidase, and of 35 and 36 kDa, if deglycosylated with N-glycanase or trifluoromethanesulfonic acid. Affinity purified rabbit antibodies against each KSPG recognized only the intact proteoglycan or its core proteins in immunoblots of unfractionated guanidine-HCl extracts of whole cornea after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Affinity purified antibody to a synthetic peptide duplicating the NH2-terminal sequence of the 37-kDa bovine core protein showed little reactivity with untreated corneal extract but reacted with the 47-kDa bovine protein in endo-beta-galactosidase-treated extracts. RNA was isolated from bovine and chick corneal stromas and used for in vitro translation. Antibody against bovine KSPG immunoprecipitated two proteins of 56-53 kDa and a protein of 41 kDa after translation of bovine RNA. Translation of chick RNA produced a double band of 38-39 kDa and a single band of 25 kDa precipitating with antibody against chicken KSPG. Homologous unlabeled KSPG competed for binding of antibodies to these translation products. These data suggest that in vertebrate corneas, the multiple KSPG core protein isoforms may arise as products of separate mRNAs, rather than from proteolytic processing of a large polypeptide precursor.
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PMID:Cell-free translation and characterization of corneal keratan sulfate proteoglycan core proteins. 171 81

Human activation inducer molecule (AIM/CD69), a dimeric glycoprotein structure of 33 and 27 kDa, is the earliest inducible cell surface antigen expressed during lymphocyte activation and is implicated in the induction of T and B cell proliferative responses. Cross-competition monoclonal antibodies (mAb) binding assays have allowed the definition of four antigenic epitopes. Three of them (antigenic sites E1-3) are extracellular while the fourth (site I) is a sequential epitope localized intracellularly and highly conserved interspecies. Site E1 is shown to be an immunodominant antigenic determinant closely related to a functional domain of AIM important for triggering of T cell proliferation. Studies of peptide fragmentation of the two isolated AIM subunits with different proteases have demonstrated that both AIM chains are differentially glycosylated forms of a single 24-kDa core protein. Moreover, the two denatured and isolated AIM chains share common epitope(s) as demonstrated by their reactivity with an mAb by both Western blot analysis and immunoprecipitation of the separated AIM subunits. Biosynthesis studies revealed the rapid appearance of two intermediate precursor forms of 29 and 26 kDa which arise from the 24-kDa unglycosylated AIM polypeptide. This 24-kDa unglycosylated form could be also precipitated from iodinated cells pretreated with tunicamycin, indicating that glycosylation of the protein was neither required for AIM cell surface expression nor for acquisition of external epitopes E1-E3. Cell treatment with pronase resulted in the loss of the external epitopes E1-3 and the generation of a proteolytic peptide of 16 kDa that could be precipitated by the anti-AIM mAb specific for the internal site I. This proteolytic fragment retained the transmembrane and cytoplasmic regions of the molecule where both epitope I and phosphorylation sites reside. These results demonstrate that AIM is an integral membrane homodimeric glycoprotein with a large cytoplasmic domain probably involved in the activation signals transduced through this molecule to lymphocytes.
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PMID:Structure-function relationship and immunochemical mapping of external and intracellular antigenic sites on the lymphocyte activation inducer molecule, AIM/CD69. 171 81

Changes in the steady-state levels of mRNAs for the alpha 1(IX) and alpha 2(IX) polypeptide chains of cartilage-characteristic type IX collagen were examined during the course of chick limb chondrogenesis in vitro and in vivo. Cytoplasmic type IX collagen mRNAs begin to accumulate at the onset of overt chondrogenesis in high density micromass culture coincident with the crucial condensation phase of the process, in which prechondrogenic mesenchymal cells become closely juxtaposed prior to depositing a cartilage matrix. The initiation of type IX collagen mRNA accumulation at condensation coincides with the initiation of accumulation of cartilage proteoglycan core protein mRNA and with a striking increase in type II collagen mRNA accumulation. Following condensation in vitro, there is a concomitant progressive increase in cytoplasmic type IX collagen, core protein, and type II collagen mRNA levels which parallels the progressive accumulation of cartilage matrix. Type IX collagen mRNAs also begin to accumulate at the initiation of overt chondrogenesis in vivo in the chondrogenic central core of the developing limb bud. In contrast, little, or no type IX collagen mRNAs are detectable in the nonchondrogenic peripheral regions of the developing limb bud.
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PMID:Type IX collagen gene expression during limb cartilage differentiation. 192 54

A recombinant baculovirus expression vector was constructed to express the core (capsid) protein of the hepatitis B virus. Along with the expected 21-kDa polypeptide, a second 24-kDa protein was observed. Immunoprecipitation and immunoblotting using a rabbit polyclonal anticore antiserum demonstrated that the two proteins were related. The core gene originally was cloned in-frame with the polyhedrin initiator codon that had been altered to AUU as a means of preventing fusion protein formation. A transient expression assay revealed expression of the 24-kDa protein was prevented if a frame-shift mutation was created upstream of the HBV core translation start site. These results suggest that the 24-kDa protein was the result of an unexpectedly high level of translation initiation at the AUU codon that gave rise to a polyhedrin-HBV core fusion protein. The 24-kDa core protein was shown to be a polyhedrin fusion protein by immunoblotting with an antipolyhedrin antiserum, and initiation at the AUU was demonstrated by amino terminal protein sequencing. Methods to prevent undesired fusion protein expression using this or similar vectors are discussed.
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PMID:Polyhedrin initiator codon altered to AUU yields unexpected fusion protein from a baculovirus vector. 193 Oct 38

A DNA fragment, coding for hepatitis core antigen (HBcAg), was amplified by polymerase chain reaction and inserted into a lambda PL promoter-derived expression vector. The recombinant plasmid was transformed into Escherichia coli and proteins produced after heat induction were analyzed. In addition to the 21 kDa HBcAg protein, several smaller related polypeptides, particularly one of 17 kDa in size, were also detected with rabbit anti-HBcAg antiserum. Whether the protease-like sequence of core protein involved in the self-cleavage process to form the 17 kDa polypeptide was investigated by a deletion experiment. Our results with a mutant in which 7 amino acids of the conserved protease-like region in the core protein have been deleted suggest that the cleavage does not depend on the presence of these protease-like sequence. In addition, the core protein synthesized from in vitro translation reaction was not cleaved. Core particles from E. coli lysate were purified by sucrose and cesium chloride density gradient centrifugations and subsequently treated with 0.2% of SDS and 0.2% of beta-mecaptoethanol. Immunoblotting analysis, however, did not reveal any conversion of the 21 kDa protein to smaller ones. In conclusion, our results suggest that the protease-like domain at the N-terminus of the core protein does not contain intrinsic autocleavage activity, nor could the HBcAg be converted to smaller antigens by detergent treatment.
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PMID:Protease-like sequence in hepatitis B virus core antigen is not involved in the cleavage processes of core protein in Escherichia coli. 193 70

Sindbis virus consists of a nucleocapsid core surrounded by a lipid membrane through which penetrate 80 glycoprotein trimers. The structure of the core protein comprising the coat surrounding the genomic RNA has been determined. The polypeptide fold from residue 114 to residue 264 is homologous to that of chymotrypsin-like serine proteinases with catalytic residues His 141, Asp 163 and Ser 215 of the core protein positioned as in other serine proteinases. The C-terminal tryptophan remains in the P1 substrate site subsequent to the autocatalytic cis cleavage of the capsid protein, thus rendering the proteinase inactive. Model building of the Sindbis core protein dimer shows that the nucleocapsid is likely to have T = 4 quasisymmetry.
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PMID:Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. 194 64

We have analysed the expression of HBV envelope (large, middle, major) and nucleocapsid (core and precore) proteins in human skin fibroblasts and Epstein-Barr virus-transformed human B-cell lines infected with recombinant vaccinia virus vectors. The large envelope protein was not secreted and barely detectable in the cytosol, whereas middle s and major s where both water soluble and efficiently secreted in abundant quantities. The precore polypeptide was also secreted whereas the core protein was totally retained within a water soluble intracellular compartment, thus confirming the presence of a signal peptide within the precore region responsible for targeting the protein to the endoplasmic reticulum for excretion. It is anticipated that such recombinants will provide a useful tool for analysis of HBV-specific cytolytic T lymphocytes.
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PMID:Expression of HBV envelope and nucleocapsid proteins in human cells using vaccinia virus vectors. 196 5

Gene 22 of bacteriophage T4 encodes a major prohead scaffolding core protein of 269 amino acid residues. From its nucleotide sequence the gene product (gp) 22 has a predicted Mr of 29.9 and a pI of 4.3. The protein is rich in charged residues (glutamic acid and lysine) and contains low amounts of proline and glycine and no cysteine residues. We suggest that gp22 undergoes limited proteolytic processing which eliminates the short C-terminal piece from the molecule during the early steps of prohead assembly. Most amino acid residues of the gp22 polypeptide chain (80%) have an alpha-helical conformation and form seven peculiar alpha-helices. A model suggesting the spatial organization of gp22 is presented. Three long alpha-helices numbered 1 (1A and 1B), 3, and 5 (5A and 5B) are packed in an antiparallel fashion along the major axis of the road-shaped molecule. Two rather short alpha-helices (2 and 4) are located at the distal and proximal ends of the protein molecule, respectively. Helix number 2, which is a proteolytic fragment of gp22 found in mature T4 heads, is packed with helices 1A and 3, similar to a novel element of supersecondary structure, the alpha alpha-corner. Helix number 4 probably interacts with the gp20 connector of the prohead. The implications of the structure of the gp22 molecule for the assembly of the prohead core are discussed.
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PMID:A proposed structure of bacteriophage T4 gene product 22--a major prohead scaffolding core protein. 208 48


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