PMID- 27165163
OWN - NLM
STAT- MEDLINE
DCOM- 20171204
LR  - 20201209
IS  - 1873-4286 (Electronic)
IS  - 1381-6128 (Linking)
VI  - 22
IP  - 33
DP  - 2016
TI  - How the Protein Architecture of RNases III Influences their Substrate 
      Specificity?
PG  - 5065-5071
AB  - BACKGROUND: The Ribonuclease III (RNase III) enzymatic class is involved in many 
      important biological processes from bacteria to higher eukaryotes. Consequently, 
      they have been useful as drug-target candidates for drug development. Despite 
      their high molecular diversity, RNases III share common structural and catalytic 
      features and some degree of enzymatic activity. However, the role of accessory 
      domains as key determinants of substrate selectivity and over the biological 
      function of each RNase III type is still under study. RESULTS: The in vitro 
      enzymatic activity of three RNase III members from class I (Escherichia coli 
      RNase III, Schizosaccharomyces pombe Pac1 and Saccharomyces cerevisiae Rntp1) and 
      the human Drosha placed in class II was revisited against four different 
      substrates. These two RNase III classes comprise members showing different domain 
      organization. Enzymatic activity differences were found among members of the 
      class I, which were even higher when the human Drosha (class II) was tested. The 
      substrate promiscuity of the E. coli RNase III was corroborated in vivo through 
      its expression in S. cerevisiae, as reported previously, but was extended here to 
      Pichia pastoris. The putative molecular mechanisms contributing for the lethal 
      effect of the heterologous RNase III on the yeast lives were deeply discussed. 
      CONCLUSION: The new generated biochemical data integrated with previous available 
      information affirmed that RNases III substrate specificity as well as their 
      cellular biological role is highly influenced by its protein structure 
      architecture. This fact also allowed drawing evolutionary links between RNase III 
      members from their structural and substrate specificity differences.
FAU - Aguero-Chapin, Guillermin
AU  - Aguero-Chapin G
FAU - Perez-Machado, Gisselle
AU  - Perez-Machado G
FAU - Mull, Juan Colli
AU  - Mull JC
FAU - Ancede-Gallardo, Evys
AU  - Ancede-Gallardo E
FAU - Antunes, Agostinho
AU  - Antunes A
FAU - Riva, Gustavo A de la Riva de la
AU  - Riva GA
AD  - Departamento de Biologia, Instituto Tecnologico Superior de Irapuato (ITESI), 
      Carretera Irapuato-Silao Km. 12.5, El Copal, Irapuato, Guanajuato, 36821, Mexico. 
      gudelariva@itesi.edu.mx.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United Arab Emirates
TA  - Curr Pharm Des
JT  - Current pharmaceutical design
JID - 9602487
RN  - EC 3.1.26.3 (Ribonuclease III)
SB  - IM
MH  - Animals
MH  - Escherichia coli/enzymology
MH  - Humans
MH  - Ribonuclease III/chemistry/*metabolism
MH  - Saccharomyces cerevisiae/enzymology
MH  - Schizosaccharomyces/enzymology
MH  - Substrate Specificity
EDAT- 2016/05/12 06:00
MHDA- 2017/12/05 06:00
CRDT- 2016/05/12 06:00
PHST- 2016/04/22 00:00 [received]
PHST- 2016/05/10 00:00 [accepted]
PHST- 2016/05/12 06:00 [pubmed]
PHST- 2017/12/05 06:00 [medline]
PHST- 2016/05/12 06:00 [entrez]
AID - CPD-EPUB-75612 [pii]
AID - 10.2174/1381612822666160511150416 [doi]
PST - ppublish
SO  - Curr Pharm Des. 2016;22(33):5065-5071. doi: 10.2174/1381612822666160511150416.