corrigendum

Dharam Singh — 2011-06-09T05:43:32Z

This corrigendum corrects Table 1 on page 3. During the preparation of the original manuscript, we mistakenly indicated that RNase II and RNase III are essential for cell survival by placing the word ¿Yes¿ in the second column of Table 1. As inactivation of only RNase II (see ref. 24) or RNase III (see Talkad, V., Achord, D. and Kennell, D. (1978) J. Bacteriol. 135: 528-541; Wang, W. and Bechhofer, D.H. (1997) J. Bacteriol. 179: 7379-7385) per se does not abolish E. coli and B. subtilis growth (i.e. two major model organisms primarily used to previously assess the importance of individual ribonucleases in bacterial mRNA turnover), the word ¿Yes¿ in the second column of Table 1 should be read as ¿No¿ in both cases. In addition, as only RNase J1 (but not RNase J2) is essential in B. subtilis for cell survival (Kobayashi et al. (2003) Proc. Natl. Acad. Sci. USA 100: 4678¿4683), the word ¿Yes¿ in the second column of the second part of Table 1 (i.e. Exoribonucleases) should be read as ¿RNase J1/Yes¿.

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

Tian-Huey Lu — 2011-06-09T05:42:48Z

It is a very good article. It is really not easy for my student, Jack, who can finish such a valuable paper in Taiwan.

We found that Asn200 of abrin-a may form a critical hydrogen bond with G4323 of 28SRNA, while corresponding Pro199 of agglutinin is a kink hydrophobic residue bound with the cleft in a more compact complementary relationship.

The reason for the lower toxicity of agglutinin than abrin-a might be due to the deformation from inactive to active state of abrin.

Journal of Biomedical Science - Latest Comments

corrigendum

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure