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)

A series of deletions, Mu insertions and point mutations affecting the malK-lamB operon have been isolated. They were used to establish a deletion map of this operon, which could be divided in 27 intervals, with 16 in malK and 11 in lamB. One interesting feature of this map is the lack of randomness in the distribution of Mu insertions in the lamB gene; by using data published elsewhere on the physical length of the deletion intervals it can be concluded that about 25% of these Mu insertions are clustered in a segment representing 2 to 8% of the gene. This map is presently being used to study the biosynthesis, structure, and function of the lamB product, which is an outer membrane protein involved in the transport of maltose and maltodextrin, and which in addition constitutes the receptor for phage lambda.
Mol Gen Genet 1979 Jul 24
PMID:Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon. 38 66

capR (lon) mutants of Escherichia coli K-12 are mucoid on minimal agar because they produce large quantities of capsular polysaccharide. When such mutants are transformed to tetracycline resistance by plasmid pMC44, a hybrid plasmid that contains a 2 megadalton (Mdal) endonuclease EcoR1 fragment of E. coli K-12 DNA joined to the cloning vehicle-pSC101, capsular polysaccharide synthesis is inhibited and the transformed colonies exhibit a non-mucoid phenotype. Re-cloning of the 2 Mdal EcoR1 fragment onto plasmid pHA105, a min-colE1 plasmid, yielded plasmid pFM100 which also inhibited capsular polysaccharide synthesis in the capR mutants. A comparison of the polypeptides specified by both plasmids pFM100 and pMC44 in minicells demonstrated that seven polypeptide bands were specified by the 2 MDal DNA, one of which was previously demonstrated to be outer membrane protein a; also known as 3b or M2 (40 kilodaltons, Kdal). Plasmid mutants no longer repressing capsular polysaccharide synthesis were either unable to specify the 40 Kdal outer membrane protein a or were deficient in synthesis of 25 Kdal and 14.5 Kdal polypeptides specified by the 2 Mdal DNA fragments. Studies with a minicell-producing strain that also contained a capR mutation indicated that the capR gene product regulated processing of at least one normal protein, the precursor of outer membrane protein a.
Mol Gen Genet 1979 Oct 01
PMID:Outer membrane protein a and other polypeptides regulate capsular polysaccharide synthesis in E. coli K-12. 39 32

Calf lens fiber cells contain a population of polyribosomes that direct, at least in vitro, the synthesis of a specific plasma membrane protein MP26. This protein may serve as a marker in terminal differentiation, since it is absent in the lens epithelium but appears in lens fiber plasma membranes. The MP26 manufacturing polyribosomes are found to be associated with a structural complex in which also the cytoskeleton and plasma membranes participate. They can be released from the complex by treatment with DNAse I. This result presumably reflects the involvement of actin in the linkage of the MP26 synthesizing polyribosomes to the cytoskeleton-membrane complex.
Mol Biol Rep 1979 May 31
PMID:Is the cytoskeleton-plasma membrane complex involved in lens protein biosynthesis? 46 Jan 86

Over sixty EMS induced mutations affecting gene lamB, presumably the structural gene for the lambda receptor in Escherichia coli K12, were examined for growth of lambda host range mutants and effect of nonsense suppressors. By the first criterion the mutations could be grouped in three classes. Bacteria with class I mutations allow growth of lambda mutants with extended host range (noted lambdah) of the type already described (Appleyard, MacGregor and Baird, 1956). Bacteria with class II mutations allow growth of lambdah mutants with still more extended host range (noted lambdahh). No host range mutants of lambda could be found which would grow on bacteria with class III mutations. Using nonsense suppressors it was found that class I and II consist of missense mutations, while class III consists of nonsense mutations. Exceptions are likely to exist (especially in class III) but were not found among the mutations tested. These observations are briefly discussed in terms of outer membrane protein integration and of phage receptor interaction.
Mol Gen Genet 1976 May 07
PMID:lamB mutations in E. coli K12: growth of lambda host range mutants and effect of nonsense suppressors. 77 86

Two F- mutants deficient in conjugation with F-type donors are isolated and characterized. Phenotypically, these mutants are similar; they have heptose-less lipopolysaccharide and lack some outer membrane protein. Genotypically, they are different. One mutant harbors a point mutation in the 70 to 74 min region, while the other is deleted for the chromosomal region 6.5 to 8.5 min. Comparison of the properties of the conjugation-deficient mutants described in this paper with other such mutants suggests that an outer membrane protein is the receptor for the f-pilus.
Mol Gen Genet 1976 Jul 05
PMID:Conjugation deficient E. coli K12 F- mutants with heptose-less lipopolysaccharide. 78 7

(1) Preparative dodecyl sulfate gel electrophoresis of human erythrocyte membrane proteins has been used to isolate dodecylsulfate band 3 containing the M,N-glycoprotein and the major "intrinsic" membrane protein (Fairbanks, G., Steck, T.L. and Wallach, D.F.H. (1971) Biochemistry 10, 2606-2617; Bretscher, M.S. (1971) J. Mol. Biol. 59,351-357; Bretscher, M.S. (1971) Nat. New Biol. 231, 229-232 and Marchesi, V.T. and Andrews, E.P. (1972) Science 174, 1247-1248). Subsequent isoelectric focusing in polyacrylamide gels containing Triton X-100 separates these two entities and allows their simultaneous purification. (2) The proteins thus obtained retain their antigenic properties. They are pure according to electrophoretic and immunoelectrophoretic criteria. However, crossed immunoelectrophoresis yields evidence for molecular microheterogeneity of the major "intrinsic" protein. (3) Analyses utilizing crossed immunoelectrophoresis with antibodies absorbed with intact erythrocytes show that the major "intrinsic" protein possesses antigenic determinants on both membrane surfaces and therefore spans the erythrocyte membrane. All determinants of the M,N-glycoprotein detectable with our antibodies were found solely on the exterior membrane surface. (4) Neither the major "intrinsic" membrane protein nor the major M,N-glycoprotein bound significantly to concanavalin A in crossed immunoaffinoelectrophoresis.
 ...
PMID:The major "intrinsic" membrane protein of human erythrocytes. Preparative isolation and immunoelectrophoretic analyses. 99 Feb 85

The messenger RNAs for the outer membrane proteins in E. coli are more stable than the bulk of the messenger RNA s (Hirashima et al., 1973). Polysomes, enriched in those containing stable mRNAs have been isolated following rifampicin treatment and have been shown to contain quantitatively the same complement of ribosomal protein as normal polysomes. There is one exception: ribosomal protein S1 is present in larger amounts in the polysomes containing stable messengers. However, there are grounds for believing this finding to be an artifact. It is concluded that the differences between outer membrane protein synthesis and bulk protein synthesis are not due to a difference in the ribosomes.
Mol Gen Genet 1975
PMID:Analysis of the ribosomes engaged in the synthesis of the outer membrane proteins of Escherichia coli. 110 14

E. coli minicells lack DNA, yet they make protein, the synthesis of which is sensitive to chloramphenicol but insensitive to rifamycin. This protein is coded for by very stable cellular mRNA with an estimated half-life of 40-80 min. In an R factor-containing minicell, two very different species of mRNA are observed: (i) R factor-specific mRNA with a short half-life whose synthesis is rifamycin-sensitive and (ii) cellular mRNA with a long half-life whose synthesis is rifamycin-insensitive. These findings indicate that minicells contain normal degradative mechanisms for mRNA and point out the existence of a unique class of very stable cellular mRNA. Greater than 80% of the rifamycin-insensitive protein synthesized goes into the outer minicell membrane. Relatively stable mRNA, half-life 5.5-11.5 min, for outer membrane protein in whole cells has been reported [Hirashima et al. (1973) J. Mol. Biol. 79, 373-389]. The stability of minicell mRNA is significantly greater. This and other observations suggest that there are two functional species of mRNA for outer membrane protein perhaps in different sites in the cell. Furthermore, these studies suggest that a class of cellular proteins is synthesized in bacteria without concomitant transcription and in the absence of association with chromosomal DNA.
 ...
PMID:Very stable prokaryotic messenger RNA in chromosomeless Escherichia coli minicells. 110 25

A CpG island 30 kb 3' to the human factor VIII gene in Xq28 is associated with a 2-kb transcript. This gene encodes a previously described palmitoylated membrane protein, p55, containing a src homology motif, SH3. Although originally described in reticulocytes, the transcript is expressed in a wide variety of human tissues. The gene is also present in the mouse and expressed in all mouse tissues examined. No known factor VIII gene deletions extend into the p55 gene. Since the function of the p55 protein is not known, the p55 gene is formally a candidate for any of the 19 or more disease genes that have not been isolated but are closely linked genetically to the factor VIII gene.
Hum Mol Genet 1992 May
PMID:The gene encoding the palmitoylated erythrocyte membrane protein, p55, originates at the CpG island 3' to the factor VIII gene. 130 Nov 63

Glucose uptake by brown adipose tissue, measured following deoxyglucose injection in vivo, was increased by 6- and 11-fold following 2 and 14 days of cold exposure, respectively. To look for the possible mechanism of these modifications, the glucose transporter Glut 4 has been characterized at the protein and mRNA levels in brown adipose tissue, skeletal muscle and white adipose tissue following cold acclimation. Crude membranes were prepared from those tissues, and Glut 4 was studied by Western blot analysis. In brown adipose tissue, the total Glut 4 amount was increased by 52 +/- 7% and by 104 +/- 12% following 2 and 14 days of cold exposure, respectively. By contrast, in white adipose tissue of 14-day-cold-exposed mice the total Glut 4 content was decreased by 42 +/- 5%. However, Glut 4 concentration, expressed per mg of membrane protein, was unchanged in both brown and white adipose tissues following cold exposure, since the membrane protein content increased in brown but decreased in white adipose tissue. No modification in Glut 4 content was observed in skeletal muscle from cold-exposed mice. Total RNA were prepared and analyzed for Glut 4, glyceraldehyde phosphate dehydrogenase (GAPDH) and actin. Glut 4 and GAPDH mRNA were increased 2-fold in brown adipose tissue from cold-exposed mice, while actin mRNA content was unmodified. Glut 4 mRNA content was not changed in white adipose tissue and skeletal muscle from cold-exposed mice. Our results suggest that Glut 4 expression is differently modulated in the three insulin-responsive tissues during cold acclimation.
Mol Cell Endocrinol 1992 Nov
PMID:Effect of cold acclimation on the expression of glucose transporter Glut 4. 130 80


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