Chapter 773 UmuD and UmuD′ Proteins

نویسنده

  • John W. Little
چکیده

Escherichia coli. Cell 29, 11 22. [17] Friedberg, E.C., Walker, G.C., Siede, W., Wood, R.D., Schultz, R.A., Ellenberger, T. (2005). DNA Repair and Mutagenesis, 2nd edn, Washington, DC: American Society of Microbiology Press. [18] Sassanfar, M., Roberts, J.W. (1990). Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication. J. Mol. Biol. 212, 79 96. [19] Ptashne, M. (2004). A Genetic Switch: Phage Lambda Revisited, 3rd edn., Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. [20] Yang, W., Woodgate, R. (2007). What a difference a decade makes: Insights into translesion DNA synthesis. Proc. Natl. Acad. Sci. USA 104, 15591 15598. [21] Roland, K.L., Smith, M.H., Rupley, J.A., Little, J.W. (1992). In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. J. Mol. Biol. 228, 395 408. [22] Chen, Z., Yang, H., Pavletich, N.P. (2008). Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 453, 489 496. [23] Story, R.M., Weber, I.T., Steitz, T.A. (1992). The structure of the E. coli recA protein monomer and polymer. Nature 355, 318 325. [24] Kim, B., Little, J.W. (1993). LexA and λ CI repressors as enzymes: specific cleavage in an intermolecular reaction. Cell 73, 1165 1173. [25] Giese, K.C., Michalowski, C.B., Little, J.W. (2008). RecA-dependent cleavage of LexA dimers. J. Mol. Biol. 377, 148 161. [26] Gimble, F.S., Sauer, R.T. (1989). Lambda repressor mutants that are better substrates for RecA-mediated cleavage. J. Mol. Biol. 206, 29 39. [27] Paetzel, M., Strynadka, N.C J. (1999). Common protein architecture and binding sites in proteases utilizing a Ser/Lys dyad mechanism. Protein Sci. 8, 2533 2536.

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Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis.

The products of the SOS-regulated umuDC operon are required for most UV and chemical mutagenesis in Escherichia coli. The UmuD protein shares homology with a family of proteins that includes LexA and several bacteriophage repressors. UmuD is posttranslationally activated for its role in mutagenesis by a RecA-mediated proteolytic cleavage that yields UmuD'. A set of missense mutants of umuD was ...

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Targeting of the UmuD, UmuD', and MucA' mutagenesis proteins to DNA by RecA protein.

In addition to its critical role in genetic recombination, the Escherichia coli RecA protein plays a pivotal role in SOS-induced mutagenesis. This role can be separated genetically into three steps: (i) depression of the SOS regulon by mediating the posttranslational cleavage of the LexA repressor, (ii) activation of UmuD'-like proteins by mediating cleavage of the UmuD-like proteins, and (iii)...

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Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage.

Most translesion DNA synthesis (TLS) in Escherichia coli is dependent upon the products of the umuDC genes, which encode a DNA polymerase, DNA polymerase V, with the unique ability to replicate over a variety of DNA lesions, including cyclobutane dimers and abasic sites. The UmuD protein is activated for its role in TLS by a RecA-single-stranded DNA (ssDNA)-facilitated self-cleavage event that ...

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Regulation of E . coli SOS Mutagenesis by Dimeric Intrinsically Disordered umuD Gene Products

Products of the umuD gene in E. coli are involved in regulating the timing of error-free DNA repair processes and mutagenic translesion DNA synthesis (TLS) during the SOS response to DNA damage. Homodimeric UmuD2 is upregulated early during the SOS response, and a slow post-translational autocleavage process removes the N-terminal 24 amino acids of each UmuD monomer. The remaining C-terminal fr...

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Altering the N-terminal arms of the polymerase manager protein UmuD modulates protein interactions

Escherichia coli cells that are exposed to DNA damaging agents invoke the SOS response that involves expression of the umuD gene products, along with more than 50 other genes. Full-length UmuD is expressed as a 139-amino-acid protein, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. The N-terminal arms of UmuD are dynamic and contain recognition sites for multiple partner p...

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Regulation of SOS mutagenesis by proteolysis ( UmuD / D ' / UmuC / Lon / ClpXP / protein - protein interactions )

DNA damage-inducible mutagenesis in Escherichia coli is largely dependent upon the activity of the UmuD (UmuD') and UmuC proteins. The intracellular level of these proteins is tightly regulated at both the transcriptional and the posttranslational levels. Such regulation presumably allows cells to deal with DNA damage via error-free repair pathways before being committed to error-prone pathways...

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تاریخ انتشار 2012