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N gene product

Similarly, when termination at a site within an operon or at the end of a leader region is affected by a specific regulatory signal, an efficient control can be achieved. One of the most studied controls over a p-dependent termination is that which occurs at the XtRl site and is prevented by the X N gene product... [Pg.81]

Like the activity of p Itself, the activity of the N gene product is dependent on the elongation subunit of RNA polymerase specified by the E. aoti nusA gene. It might be anticipated that attenuation of transcription by a specific antiterminating protein is a general pattern that will be found to occur frequently in microbial systems. [Pg.81]

Alestrom, P., Akusjarvi, G., Pettersson, M., and Pettersson, U., 1982, DNA sequence analysis of the region encoding the terminal protein and the hypothetical N-gene product of adenovirus type 2, J. Biol. Chem. 257 13492. [Pg.346]

ECEs are metalloproteinases that are homologous to the neutral endopeptidase (NEP, E-24.11, neprilysin) unlike NEP, however, they form disulfide-bonded homodimers. In man, with ECE-1 and ECE-2, two isoforms are known, which are encoded by two separate genes. For ECE-1 four different variants have been identified (ECE-1 a-d), which are generated by the use of alternative promoters (Table 2). The ECE-1 isoforms only differ in their N-terminal amino acid sequence. For ECE-2, a single gene product has been described in... [Pg.471]

Misawa, N. et al.. Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli, J. Bacteriol. 172, 6704, 1990. [Pg.392]

Misawa, N. et al.. Expression of a tomato cDNA coding for phytoene synthase in Escherichia coli, phytoene formation in vivo and in vitro, and functional analysis of the various truncated gene products, J. Biochem. (Tokyo) 116, 980, 1994. [Pg.395]

Youssef S, Maor G, Wildbaum G, Grabie N, Gour-Lavie A, Karin N. C-C chemokine-encoding DNA vaccines enhance breakdown of tolerance to their gene products and treat ongoing adjuvant arthritis. J Clin Invest 2000 106(3) 361-371. [Pg.187]

Winston N J 1997 Stability of cyclin B protein during meiotic maturation and the first mitotic cell division in mouse oocytes. Biol Cell 89 211-219 Winston NJ, Maro B 1995 Calmodulin-dependent protein kinase II is activated transiently in ethanol-stimulated mouse oocytes. Dev Biol 170 350-352 Winston NJ, Bourgain-Guglielmetti F, Ciemerych MA et al 2000 Early development of mouse embryos null mutant for the cyclin A2 gene occurs in the absence of maternally derived cyclin A2 gene products. Dev Biol 223 139-153... [Pg.89]

H. J., Pinedo, H. M., Feller, N., Dekker, H., Lankelma, J., Giaccone, G., Cortisol is transported by the multidrug resistance gene product... [Pg.442]

Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., and Candey, L. C. (2002). Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10, 151—162. [Pg.174]

Pellizzoni, L., Kataoka, N., Charroux, B. and Dreyfuss, G. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing. Cell 95 615-624, 1998. [Pg.628]

One important function of DUBs is the processing of ubiquitin or ubiquitin-like proteins to their mature forms. Ubiquitin is expressed in cells as either linear poly-ubiquitin or N-terminally fused to certain ribosomal proteins [79, 80]. These gene products are processed by DUBs to separate the ubiquitin into monomers and expose the gly-gly motif at the G-terminus. Many DUBs process linear polyubiquitin or Ub-fusion proteins in vitro, but this processing appears to take place cotransla-tionally in vivo and is extremely rapid. This makes analysis difficult and leaves unanswered the question of which DUBs actually perform this function in vivo. Multiple DUBs may be able to perform this processing at a physiologically relevant level since DUB deletions rarely shows processing defects [81]. [Pg.203]

Figure 4.1 Nickel transport in . co//.The lower part of the figure shows the nik gene cluster from coli which encodes a nickel specific ABC-type transporter and the repressor protein (NikR).The likely roles of the various nik gene products are indicated in the upper part of the figure.The transporter is encoded by the nikBCDE genes whilst a periplasmic nickel-binding protein is encoded by n/M.The system is expressed when nickel is low. High nickel represses expression via NikR and under these conditions nickel is transported via the Mg transporter (top left). Figure 4.1 Nickel transport in . co//.The lower part of the figure shows the nik gene cluster from coli which encodes a nickel specific ABC-type transporter and the repressor protein (NikR).The likely roles of the various nik gene products are indicated in the upper part of the figure.The transporter is encoded by the nikBCDE genes whilst a periplasmic nickel-binding protein is encoded by n/M.The system is expressed when nickel is low. High nickel represses expression via NikR and under these conditions nickel is transported via the Mg transporter (top left).
Rentsch, J., Levens, N., and Chiesi, M. (1995) Recombinant ob-gene product reduces food intake in fasted mice. Biochem. Biophys. Res. Commun. 214, 131-136. [Pg.391]

N-terminal sequencing of the two polypeptides present in spinach and barley LHCI-730 allowed their identification with Lhcal and LhcaA gene products... [Pg.159]

The first indication that modification of specific tail residues were linked to chromatin functional states, came from immunostaining of Drosophila polytene chromosomes with antibodies specific for H4 acetylated at defined lysines [13]. As shown in Fig. 2A, H4 acetylated at lysine 16 (H4acK16) was found almost exclusively on the transcriptional hyperactive male X chromosome (Fig. 2). (Genes on the Drosophila male X are transcribed twice as fast as their female counterparts so as to equalize levels of X-linked gene products between XY males and XX females.) In addition, H4 lysine 12 was found to remain acetylated in centric heterochromatin, while lysines 5, 8, and 16 were all under-acetylated [13]. These observations led to the suggestion that the histone N-terminal tails constitute nucleosome surface markers that can be recognized by non-histone proteins in a modification-dependent manner to alter the functional state of chromatin [13]. [Pg.293]


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See also in sourсe #XX -- [ Pg.81 ]




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