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...
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Comment on: Kaberdin et al. Journal of Biomedical Science, 18:23
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, 09 June 2011)
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. read full comment
Comment on: Cheng et al. Journal of Biomedical Science, 17:34
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corrigendum (Dharam Singh, 09 June 2011)
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... read full comment
Comment on: Kaberdin et al. Journal of Biomedical Science, 18:23
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, 09 June 2011)
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.
read full comment
Comment on: Cheng et al. Journal of Biomedical Science, 17:34