Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0016632 (Fox)
 1,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The collagenase domain of bovine glomerular basement membrane was isolated in soluble form after limited digestion with pepsin. Gel filtration chromatography of the domain under denaturing conditions revealed that most of the polypeptide constituents exhibit apparent molecular weights greater than the type I collagen beta-chain, while approximately 15% are similar in size to that of alpha-chain. Carboxymethyl cellulose chromatography of the alpha-size region revealed that 70% of the protein was polypeptide XIV, as previously designated (West, T. W., Fox, J. W., Jodlowski, M., Freytag, J. W., and Hudson, B. G. (1980) J. Biol. Chem. 255, 10451-10459). This polypeptide exhibits an apparent molecular weight of 102,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. An absolute molecular weight value of 86,000 was determined by sedimentation equilibrium ultracentrifugation in 6 M guanidine hydrochloride. About 15% of the mass is carbohydrate which exists in the form of glucosylgalactosylhydroxylysine. Thus, the polypeptide backbone has a molecular weight of 73,000, a value which is considerably smaller than the alpha-chains of classical collagen. The amino acid and carbohydrate composition and cyanogen bromide patterns indicate that polypeptide XIV has a structure similar to that of C-chain or alpha 1 (IV) collagen which has been identified in other tissues. In addition, the cyanogen bromide pattern of the entire collagenous domain is similar to that of polypeptide XIV, suggesting that the latter is a structural segment of many of the higher molecular weight components.
 ...
PMID:Bovine glomerular basement membrane. Characterization of an alpha-size collagenous polypeptide. 725 9

In Anabaena spp., synthesis of the heterocyst envelope polysaccharide, required if the cell is to fix dinitrogen under aerobic conditions, is dependent on the gene hepA. A transcriptional start site of hepA was localized 104 bp 5' from its translational initiation codon. A 765-bp open reading frame, denoted hepC, was found farther upstream. Inactivation of hepC led to constitutive expression of hepA and prevented the synthesis of heterocyst envelope polysaccharide. However, the glycolipid layer of the heterocyst envelope was synthesized. A hepK mutation blocked both the synthesis of the heterocyst envelope polysaccharide and induction of hepA. The predicted product of hepK resembles a sensory protein-histidine kinase of a two-component regulatory system. Analysis of the region between hepC and hepA indicated that DNA sequences required for the induction of hepA upon nitrogen deprivation are present between bp -574 and -440 and between bp -340 and -169 relative to the transcriptional start site of hepA. Gel mobility shift assays provided evidence that one or more proteins bind specifically to the latter sequence. The Fox box sequence downstream from hepA appeared inessential for the induction of hepA.
 ...
PMID:Regulation of hepA of Anabaena sp. strain PCC 7120 by elements 5' from the gene and by hepK. 969 74