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Keywords: endonuclease
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Articles
Biochem J (2011) 435 (1): 103–111.
Published: 15 March 2011
...Xuhua Gan; Jing Yang; Jun Li; Haiyan Yu; Hongmei Dai; Jinyu Liu; Ying Huang tRNase Z is the endonuclease that is involved in tRNA 3′-end maturation by removal of the 3′-trailer sequences from tRNA precursors. Most eukaryotes examined to date, including the budding yeast Saccharomyces cerevisiae and...
Includes: Supplementary data
Articles
Biochem J (2009) 423 (2): 265–277.
Published: 25 September 2009
...Viswanadham Duppatla; Chiranjeevi Bodda; Claus Urbanke; Peter Friedhoff; Desirazu N. Rao The mut L gene of Neisseria gonorrhoeae has been cloned and the gene product purified. We have found that the homodimeric N. gonorrhoeae MutL (NgoL) protein displays an endonuclease activity that incises...
Includes: Supplementary data
Articles
Biochem J (2009) 422 (3): 483–492.
Published: 27 August 2009
... report that both sptrz1 + and sptrz2 + are essential for growth. Moreover, sptrz1 + is required for cell viability in the absence of Sla1p, which is thought to be required for endonuclease-mediated maturation of pre-tRNA 3′ ends in yeast. Both scTRZ1 and ELAC2 can complement a temperature-sensitive...
Includes: Supplementary data
Articles
Biochem J (2004) 380 (3): 929–937.
Published: 15 June 2004
...Markus NAPIREI; Albert RICKEN; Dirk EULITZ; Heiko KNOOP; Hans Georg MANNHERZ The tissue distribution of deoxyribonuclease 1 (DNASE1, DNase I), a Ca 2+ and Mg 2+ /Mn 2+ -dependent secretory endonuclease, has previously been investigated. However, most of these studies did not account for the...
Articles
Biochem J (2003) 371 (3): 867–876.
Published: 01 May 2003
...Kyle S. MacLEA; Ronald J. KRIESER; Alan EASTMAN DNase IIα (EC 3.1.22.1) is an endonuclease, which is active at low pH, that cleaves double-stranded DNA to short 3′-phosphoryl oligonucleotides. Although its biochemistry is well understood, its structure–activity relationship has been largely...
Articles
Biochem J (2003) 371 (2): 321–330.
Published: 15 April 2003
... poorly defined C-terminal domain. We show here that the C-terminal domain of NPP1–3 is structurally related to a family of DNA/RNA non-specific endonucleases. However, none of the residues that are essential for catalysis by the endonucleases are conserved in NPP1–NPP3, suggesting that the nuclease-like...