2009
DOI: 10.1016/j.abb.2008.10.012
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Role of the basic character of α-sarcin’s NH2-terminal β-hairpin in ribosome recognition and phospholipid interaction

Abstract: Ribotoxins are a family of toxic extracellular fungal RNases that first enter into the cells and then exert a highly specific ribonucleolytic activity on the larger rRNA molecule, leading to protein synthesis inhibition and cell death by apoptosis. α-Sarcin is the best characterized ribotoxin. Previous characterization of a deletion variant of this protein showed that its long NH 2 -terminal β-hairpin is essential for its cytotoxicity. Docking, enzymatic, and lipidprotein interaction studies suggested that thi… Show more

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Cited by 15 publications
(12 citation statements)
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“…The evolutionary distances were computed using the Poisson distribution method [40] and are in units of number of amino acid substitutions per site. Interestingly, we have also found comparable behaviours in other cytotoxic RNase families, such as the contribution of the N-terminus of ribotoxin in the interaction with lipid bilayers [34]. Evolutionary analyses were conducted in MEGA5 [41].…”
Section: Figure 3 Conservation Of the N-terminal Antimicrobial Domainmentioning
confidence: 59%
“…The evolutionary distances were computed using the Poisson distribution method [40] and are in units of number of amino acid substitutions per site. Interestingly, we have also found comparable behaviours in other cytotoxic RNase families, such as the contribution of the N-terminus of ribotoxin in the interaction with lipid bilayers [34]. Evolutionary analyses were conducted in MEGA5 [41].…”
Section: Figure 3 Conservation Of the N-terminal Antimicrobial Domainmentioning
confidence: 59%
“…Alpha-sarcin contains three discrete membrane interaction regions, one of which, the N-terminal beta hairpin, is not only required to target specific ribosomal proteins, but is also the region where many of the electrostatic interactions with the acidic membrane surface take place [67]. It is tempting to speculate that the N-terminal immunity protein binding site of the rRNase E3 which is also involved in ribosomal protein binding [68], is equally important in the membrane targeting process, given its basic nature, amphipathic character, inherent flexibility, lack of interactions with the main beta sheet and absence of membrane binding in the presence of immunity protein.…”
Section: Discussionmentioning
confidence: 99%
“…Spectroscopic characterization was performed following well-established procedures (Álvarez-García et al 2006;Álvarez-García et al 2009b;García-Ortega et al 2005a;García-Ortega et al 2001;García-Ortega et al 2002;Lacadena et al 1999;Martínez-Ruiz et al 2001). Absorbance measurements were carried out on a Beckman DU640 were also used to calculate their extinction coefficients (Table 1).…”
Section: Spectroscopic Characterizationmentioning
confidence: 99%
“…In fact, it has been reported before how α-sarcin Lys 14 and 21, with identical amino acids in equivalent positions of HtA (Fig. 1), are crucial residues for the correct achievement of these interactions (Álvarez-García et al 2009b). …”
mentioning
confidence: 99%