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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The conformation of some regular polypeptides: (Lys-Ala)50, (Lys-Ala2)37, (Lys-Ala2)26, (Lys-Ala3)18, (Lys3-Pro)29, (Orn3-Gly)28 was studied by means of CD. The complexes of these polypeptides with DNA were obtained by the methods of jump-dilution of a two-components mixture from 2 M NaCl to 0.05 M NaCl. The extent of DNA covering by the polypeptides was compared using binding isoterms of ethidium on DNA and DNA-polypeptide complex. The length, L, which polypeptides cover on DNA was estimated by means of energy transfer between the dyes absorbed on the complexes. The CD spectra of the complexes revealed a high sensitivity to changes of the environmental conditions. Small variations in the temperature and ionic strength produces marked changes in the CD spectra of the complexes. It was suggested that observed CD changes are due to both the structural relaxation of the complexes and the existence of liquid-crystal domains in solution.
Mol Biol (Mosk)
PMID:[Structure of DNA complexes with regular polypeptides]. 65 74

Internal regularities of amino acid sequences of flavodoxins, FMN-containing, low molecular weight flavoproteins, were statistically examined using the minimum mutation method. The sequence of Clostridium pasteurianum flavodoxin shows statistically significant evidence of repetitious internal gene duplications at different levels of structure. Peptide pairs with a low chance probabilitiy of occurrence were frequently observed at a shift of 5 residues. The pairs with the lowest chance probabilities are a pair of heptapeptides at positions39--45 vs. 44--50, a 5 residue shift (p = 9 x 10(-6)). Most of the related pairs are consistent and could best be explained by the repeating pentapeptide sequence: (Lys-Gly-Ala-Asp-Val-)n and appropriate gaps. Internal repetitions with longer shifts were also suggested for other flavodoxins. Repetitious gene duplication is proposed for the early stages of flavodoxin evolution.
J Mol Evol 1978 Aug 02
PMID:The evolution of protein sequences by repetitious gene duplication: clostridial flavodoxin. 69 Oct 74

Microsomes isolated from the fibroin region of the Bombyx mori silkgland synthesize in the cell-free system a glycin rich polypeptide or polypeptides presumably representing fibroin precursors. Besides microsomes the system requires ATP and ATP-generating system, GTP, soluble protein fraction and tRNA, glycine incorporation is inhibited by puromycin and cycloheximide. It is shown that the synthesis of a polypeptide with high Gly/Lys ratio requires soluble protein fraction isolated from the silk gland at the end of the instar V. When the soluble protein fraction from the larvoe at the early instar V is used the Gly/Lys ratio in the product is markedly lower. These results permit to suggest that fibroin synthesis may be regulated at the level of tRNA aminoacylation.
Mol Biol (Mosk)
PMID:[Properties of the cell-free protein synthesizing system from the fibroin region of the Bombyx mori silkgland]. 105 90

The plasma LH (luteinizing hormone) response to 200 ng of LH-RH (LH-releasing hormone) injected subcutaneously at different stages of the estrous cycle in normal rats under Surital anesthisia was maximal during the afternoon of proestrus and lowest on diestrus I. The area under the plasma LH curve measured at 13:00 on proestrus was approximately 7-fold higher than that obtained at 15:30 h on diestrus I. Intermediate responses were found on diestrus II, estrus and morning of proestrus. An approsimately 2.5-fold higher LH response was observed on proestrus than on diestrus I after injection of [D-Ala2, des Gly-NH2-10] LH-RH ethylamide at 15:00 h. That these marked changes of LH response are not secondary to interference by endogenous LH-RH, changes of the metabolism or transport of exogenous LH-RH or modification of plasma LH clearance is ascertanied by the finding of similar changes of pituitary sensitivity to LH-RH under in vitro conditions using pituitaries collected at the same stag-s of the estrous cycle. As measured both in vivo and in vitro, not only the amplitude but also the speed of LH response are maximal during the afternoon of proestrus and minimal on diestrus I.
Mol Cell Endocrinol 1975 Jan
PMID:Changes of pituitary sensitivity to LH-RH during the rat estrous cycle. 109 77

The reactions of benzoate ion and of glycine with adenosine 5-phosphorimidazolide have been investigated. Benzoate reacts first to give the anhydride, benzoyl-adenylate, which, in the presence of excess imidazole, reacts further to give the 2'- and 3'-esters of adenosine 5'-phosphate. Glycine also first attacks the imidazolide to give an anhydride, but this compound may react further either to give 2- and 3'-esters or to form peptides, depending on the reaction conditions.
J Mol Evol 1975 Jun 09
PMID:Prebiotic peptide-formation in the solid state. I. Reactions of benzoate ion and glycine with adenosine 5'-phosphorimidazolide. 117 27

1. Uncentrifuged and centrifuged rat intestinal contents were assayed for peptide hydrolase activity with glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanyl-glycine (Phe-Gly) as substrates in the absence and presence of the intestinal cytosol peptide hydrolase inhibitor p-hydroxymercuribenzoate. 2. Jejunal contents hydrolysed Gly-Phe faster than Phe-Gly. Conversely, ileal contents hydrolysed Phe-Gly faster than Gly-Phe. 3. p-Hydroxymercuribenzoate markedly inhibited jejunal peptide hydrolase activity. There was ten times as much PHMB-resistant activity towards both dipeptides in ileal contents as in jejunal contents. 4. Most of the luminal enzyme activity was present in the supernatants after centrifugation, indicating the luminal enzymes exist in the soluble form. Although the presence of soluble bacterial enzymes cannot be excluded, peptide hydrolase enzymes in jejunal contents have the characteristics of mucosal cytosol enzymes whereas enzymes in ileal contents have the characteristics of mucosal bruch border as well as cytosol enzymes.
Clin Sci Mol Med 1975 Nov
PMID:A study of intraluminal peptide hydrolase activity in the rat. 119 13

A model is suggested for the lac repressor binding to the lac operator in which the repressor polypeptide chain sequences from Gly 14 to Ala 32 and from Ala 53 to Leu 71 are involved in specific interaction with operator DNA. A correspondence between the protein and DNA sequences is found which explains specificity of the repressor binding to the lac operator. The model can be extended to describe specific binding of other regulatory proteins to DNA.
Mol Biol Rep 1976 Apr
PMID:A model for the binding of lac repressor to the lac operator. 127 66

X-PLOR modelling of collagen dimers containing Gly-Glu-Arg in each chain has been carried out. The interaction between molecules when two Gly-Glu-Arg are present on each chain is found to be substantially less than two times that obtained with one per chain, implying that relative tilting of two collagen molecules does not offset the disadvantages of misalignment of the interacting moieties. This implies that if multiple (Glu(-)-Arg+)3 interactions are important in fibril formation, their lateral separations must be large enough to insure that they act independently.
J Mol Recognit 1992 Sep
PMID:Intermolecular interactions in type I collagens. 129 4

The development of an efficient expression system for insulin-like growth factor-I (IGF-I) in Escherichia coli as a fusion protein is described. The fusion protein consists of an N-terminal extension made up of the first 46 amino acids of methionyl porcine GH ([Met1]-pGH) followed by the dipeptide Val-Asn. The latter two residues provide a unique hydroxylamine-sensitive link between [Met1]-pGH(1-46) and the N-terminal Gly of IGF-I. Downstream processing of the fusion proteins involved isolation of inclusion bodies, cleavage at the Asn-Gly bond, refolding of the reduced IGF-I peptide and purification to homogeneity. This expression system was also used to produce two variants of IGF-I in which Glu3 was substituted by either Gly or Arg to give [Gly3]-IGF-I and [Arg3]-IGF-I respectively. Production of milligram quantities of IGF-I peptide was readily achieved. The purity of the IGF-I, [Gly3]-IGF-I and [Arg3]-IGF-I was established by high-performance liquid chromatography and N-terminal sequence analysis. [Gly3]-IGF-I and [Arg3]-IGF-I were more potent than IGF-I in biological assays measuring stimulation of protein synthesis and DNA synthesis or inhibition of protein breakdown in rat L6 myoblasts. Both analogues bound very poorly to bovine IGF-binding protein-2 and slightly less well than IGF-I to the type-1 receptor on rat L6 myoblasts. We conclude that reduced binding to IGF-binding proteins rather than increased receptor binding is the likely explanation for the greater biological potency of the analogues compared with IGF-I.
J Mol Endocrinol 1992 Feb
PMID:Production and characterization of recombinant insulin-like growth factor-I (IGF-I) and potent analogues of IGF-I, with Gly or Arg substituted for Glu3, following their expression in Escherichia coli as fusion proteins. 131 30

The letA (ccdA) and letD (ccdB) genes, located just outside the sequence essential for replication of the F plasmid, apparently contribute to stable maintenance of the plasmid. The letD gene product acts to inhibit partitioning of chromosomal DNA and cell division of the host bacteria, whereas the letA gene product acts to suppress the activity of the letD gene product. To identify the target of the letD gene product, temperature-sensitive growth-defective mutants were screened from bacterial mutants that had escaped the letD product growth inhibition that occurs in hosts carrying an FletA mutant. Of nine mutants analysed, three mutants were shown, by phage P1-mediated transduction and complementation analysis, to have mutations in the gyrA gene and the other six in the groE genes. The nucleotide sequence revealed that one of the gyrA mutants has a base change from G to A at position 641 (resulting in an amino acid change from Gly to Glu at position 214) of the gyrA gene. The mutant GyrA proteins produced by these gyrA(ts) mutants were trans-dominant over wild-type GyrA protein for letD tolerance. The wild-type GyrA protein, produced in excess amounts by means of a multicopy plasmid, overcame growth inhibition of the letD gene product. These observations strongly suggest that the A subunit of DNA gyrase is the target of the LetD protein.
J Mol Biol 1992 May 05
PMID:Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit A suppress letD (ccdB) product growth inhibition. 131 44


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