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Structure, stability and aggregation propensity of a Ribonuclease A-Onconase chimera.

Abstract：

:Structural roles of loop regions are frequently overlooked in proteins. Nevertheless, they may be key players in the definition of protein topology and in the self-assembly processes occurring through domain swapping. We here investigate the effects on structure and stability of replacing the loop connecting the last two β-strands of RNase A with the corresponding region of the more thermostable Onconase. The crystal structure of this chimeric variant (RNaseA-ONC) shows that its terminal loop size better adheres to the topological rules for the design of stabilized proteins, proposed by Baker and coworkers [43]. Indeed, RNaseA-ONC displays a thermal stability close to that of RNase A, despite the lack of Pro at position 114, which, due to its propensity to favor a cis peptide bond, has been identified as an important stabilizing factor of the native protein. Accordingly, RNaseA-ONC is significantly more stable than RNase A variants lacking Pro114; RNaseA-ONC also displays a higher propensity to form oligomers in native conditions when compared to either RNase A or Onconase. This finding demonstrates that modifications of terminal loops should to be carefully controlled in terms of size and sequence to avoid unwanted and/or potentially harmful aggregation processes.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Esposito L,Donnarumma F,Ruggiero A,Leone S,Vitagliano L,Picone D

doi

10.1016/j.ijbiomac.2019.04.164

subject

Has Abstract

pub_date

2019-07-15 00:00:00

pages

1125-1133

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)31077-3

journal_volume

133

pub_type

杂志文章

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