scholarly journals Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay

2017 ◽  
Vol 7 (5) ◽  
pp. 571-582 ◽  
Author(s):  
Congjie Zhai ◽  
Ling Ma ◽  
Zhixin Zhang ◽  
Jiwei Ding ◽  
Jing Wang ◽  
...  
BMC Biology ◽  
2010 ◽  
Vol 8 (1) ◽  
pp. 17 ◽  
Author(s):  
Mohammad G Sabbir ◽  
Nichola Wigle ◽  
Shauna Loewen ◽  
Yuan Gu ◽  
Cordula Buse ◽  
...  

Microbiology ◽  
2009 ◽  
Vol 155 (9) ◽  
pp. 2930-2940 ◽  
Author(s):  
Keith E. Weaver ◽  
Shirisha G. Reddy ◽  
Cassandra L. Brinkman ◽  
Smita Patel ◽  
Kenneth W. Bayles ◽  
...  

The par locus of the Enterococcus faecalis plasmid pAD1 is an RNA-regulated addiction module encoding the peptide toxin Fst. Homology searches revealed that Fst belongs to a family of at least nine related peptides encoded on the chromosomes and plasmids of six different Gram-positive bacterial species. Comparison of an alignment of these peptides with the results of a saturation mutagenesis analysis indicated regions of the peptides important for biological function. Examination of the genetic context of the fst genes revealed that all of these peptides are encoded within par-like loci with conserved features similar to pAD1 par. All four Ent. faecalis family members were demonstrated to produce the expected toxin-encoding and regulatory RNA products. The locus from the Ent. faecalis plasmid pAMS1 was demonstrated to function as an addiction module and Fst was shown to be toxic to Staphylococcus aureus, suggesting that a plasmid-encoded module in that species is performing the same function. Thus, the pAD1-encoded par locus appears to be the prototype of a family of related loci found in several Gram-positive species.


Molecules ◽  
2021 ◽  
Vol 27 (1) ◽  
pp. 15
Author(s):  
Eduardo Fuentes-Lemus ◽  
Per Hägglund ◽  
Camilo López-Alarcón ◽  
Michael J. Davies

Covalent crosslinks within or between proteins play a key role in determining the structure and function of proteins. Some of these are formed intentionally by either enzymatic or molecular reactions and are critical to normal physiological function. Others are generated as a consequence of exposure to oxidants (radicals, excited states or two-electron species) and other endogenous or external stimuli, or as a result of the actions of a number of enzymes (e.g., oxidases and peroxidases). Increasing evidence indicates that the accumulation of unwanted crosslinks, as is seen in ageing and multiple pathologies, has adverse effects on biological function. In this article, we review the spectrum of crosslinks, both reducible and non-reducible, currently known to be formed on proteins; the mechanisms of their formation; and experimental approaches to the detection, identification and characterization of these species.


2019 ◽  
Vol 47 (18) ◽  
pp. 9480-9494 ◽  
Author(s):  
Christina E Weinberg ◽  
Zasha Weinberg ◽  
Christian Hammann

Abstract Small endonucleolytic ribozymes promote the self-cleavage of their own phosphodiester backbone at a specific linkage. The structures of and the reactions catalysed by members of individual families have been studied in great detail in the past decades. In recent years, bioinformatics studies have uncovered a considerable number of new examples of known catalytic RNA motifs. Importantly, entirely novel ribozyme classes were also discovered, for most of which both structural and biochemical information became rapidly available. However, for the majority of the new ribozymes, which are found in the genomes of a variety of species, a biological function remains elusive. Here, we concentrate on the different approaches to find catalytic RNA motifs in sequence databases. We summarize the emerging principles of RNA catalysis as observed for small endonucleolytic ribozymes. Finally, we address the biological functions of those ribozymes, where relevant information is available and common themes on their cellular activities are emerging. We conclude by speculating on the possibility that the identification and characterization of proteins that we hypothesize to be endogenously associated with catalytic RNA might help in answering the ever-present question of the biological function of the growing number of genomically encoded, small endonucleolytic ribozymes.


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