ssonδ and ssonδlong two thermostable esterases from the same orf in the archaeon sulfolobus solfataricusssonδssonδlong两个耐热性的酯酶从同样的orf archaeon硫化叶菌solfataricus.pdf

Archaea 2, 109–115 © 2006 Heron Publishing—Victoria, Canada SSoN and SsoN long: two thermostable esterases from the same ORF in the archaeon Sulfolobus solfataricus? LUIGI MANDRICH,1 MARGHERITA PEZZULLO,1 MOSÈ ROSSI1 AND GIUSEPPE 1,2 MANCO 1 Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, 80131, Naples, Italy 2 Corresponding author (g.manco@r.it) Received July 14, 2006; accepted October 13, 2006; published online November 20, 2006 Summary Previously, we reported from the Sulfolobus among these proteins and sometimes by different structural or- solfataricus open reading frame (ORF) SSO2517 the cloning, ganization (De Simone et al. 2001). Recently, we cloned and overexpression and characterization of an esterase belonging characterized an esterase belonging to the HSL family from to the hormone-sensitive lipase (HSL) family and apparently Sulfolobus solfataricus P2 (She et al. 2001), which we named having a deletion at the N-terminus, which we named SsoNΔ. SsoNΔ. SsoNΔ is characterized by a large deletion at the N-ter- Searching the recently reported Sulfolobus acidocaldarius ge- minus (Mandrich et al. 2005). In parallel, we performed a nome by sequence alignment, using SSO2517 as a query, al- comparative analysis with a truncated version of another pro- lowed identity of a putative esterase (ORF SAC1105) sharing tein of the HSL family, namely, Alicyclobacillus acidocald- high sequence similarity (82%) with SSO2517. This esterase arius esterase 2 (EST2; Manco et al. 1997, 1998), and demon- displays an N-terminus and total length similar to other known strated that the N-terminus of EST2 is involved in substrate esterases of the HSL family. Analysis of the upstream DNA se- specificity, cataly