The origin of biological homochirality

Blackmond, Donna G.

doi:10.1098/rstb.2011.0130

Cited by 102 publications

(73 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…43,44 Besides that, free D-amino acids were discovered only in brain tissue. 45 We argue that a poly D-arginine peptide may not exhibit the specific binding to the same cellular target components, e.g., proteins or nucleic acids, as the L-enantiomer.…”

Section: Resultsmentioning

confidence: 99%

Principles of protein targeting to the nucleolus

Martin

Ter-Avetisyan

Herce

et al. 2015

Nucleus

114

View full text Add to dashboard Cite

The nucleolus is the hallmark of nuclear compartmentalization and has been shown to exert multiple roles in cellular metabolism besides its main function as the place of rRNA synthesis and assembly of ribosomes. Nucleolar proteins dynamically localize and accumulate in this nuclear compartment relative to the surrounding nucleoplasm. In this study, we have assessed the molecular requirements that are necessary and sufficient for the localization and accumulation of peptides and proteins inside the nucleoli of living cells. The data showed that positively charged peptide entities composed of arginines alone and with an isoelectric point at and above 12.6 are necessary and sufficient for mediating significant nucleolar accumulation. A threshold of 6 arginines is necessary for peptides to accumulate in nucleoli, but already 4 arginines are sufficient when fused within 15 amino acid residues of a nuclear localization signal of a protein. Using a pH sensitive dye, we found that the nucleolar compartment is particularly acidic when compared to the surrounding nucleoplasm and, hence, provides the ideal electrochemical environment to bind poly-arginine containing proteins. In fact, we found that oligo-arginine peptides and GFP fusions bind RNA in vitro. Consistent with RNA being the main binding partner for arginines in the nucleolus, we found that the same principles apply to cells from insects to man, indicating that this mechanism is highly conserved throughout evolution.

show abstract

Section: Resultsmentioning

confidence: 99%

Principles of protein targeting to the nucleolus

Martin

Ter-Avetisyan

Herce

et al. 2015

Nucleus

114

View full text Add to dashboard Cite

show abstract

“…1,2,15 Reaction rate equations are customarily employed to cast chemical reaction schemes in terms of coupled differential equations for the evolution of the concentrations of the species involved. In this deterministic approach, initial conditions must be taken to simulate the inherent statistical fluctuations about the ideal racemic composition.…”

Section: Introductionmentioning

confidence: 99%

Necessary conditions for the emergence of homochirality via autocatalytic self-replication

Stich

Ribó

Blackmond

et al. 2016

The Journal of Chemical Physics

Self Cite

View full text Add to dashboard Cite

We analyze a recent proposal for spontaneous mirror symmetry breaking based on the coupling of first-order enantioselective autocatalysis and direct production of the enantiomers that invokes a critical role for intrinsic reaction noise. For isolated systems, the racemic state is the unique stable outcome for both stochastic and deterministic dynamics when the system is in compliance with the constraints dictated by the thermodynamics of chemical reaction processes. In open systems, the racemic outcome also results for both stochastic and deterministic dynamics when driving the autocatalysis unidirectionally by external reagents. Nonracemic states can result in the latter only if the reverse reactions are strictly zero: these are kinetically controlled outcomes for small populations and volumes, and can be simulated by stochastic dynamics. However, the stability of the thermodynamic limit proves that the racemic outcome is the unique stable state for strictly irreversible externally driven autocatalysis. These findings contradict the suggestion that the inhibition requirement of the Frank autocatalytic model for the emergence of homochirality may be relaxed in a noise-induced mechanism. Published by AIP Publishing. [http://dx

show abstract

“…As such, we would like now to limit our consideration to just one amino acid, which we denote here as A for left enantiomer and as a for right enantiomer. We combine several well-known models described in the literature (Frank 1953;Avetisov and Goldanskii 1996;Plasson et al 2004Plasson et al , 2007Saito and Hyuga 2004;Weissbuch et al 2005;Brandenburg et al 2007;van der Meijden et al 2009;Noorduin et al 2010;Blackmond 2011;Coveney et al 2012;Hein et al 2012;Ribó et al 2013;Konstantinova 2013, 2014) and then study which combinations can possibly result in the symmetry breaking under the conditions of weak enantioselectivity of all relevant reactions. Even though the minimum interesting peptide length is three, we consider peptide chains up to length five in order to study how the increase in peptide length influences the symmetry breaking.…”

Section: Models With Peptides Up To Length 5 Catalytic Synthesis Anmentioning

confidence: 99%

“…From the third side, it was experimentally shown in (Blackmond 2011 that different properties of enantiomers and, in particular, formation of sediment of insoluble diastereomeric pairs may result in substantial enantiomeric excess (sometimes called chiral polarization) even in the absence of any autocatalysis. The application of this process to autocatalytic reactions was studied theoretically in (Konstantinov and Konstantinova 2013) where it was shown how the differences between physical properties of diastereomers may result in additional enantioselective factors.…”

Section: Introductionmentioning

confidence: 99%

“…The number of works in this area could be made a subject of a separate research. Vast number of models of chiral symmetry breaking were proposed over the years and numerous experiments were performed, for example (Frank 1953;Avetisov and Goldanskii 1996;Plasson et al 2004Plasson et al , 2007Saito and Hyuga 2004;Weissbuch et al 2005;Brandenburg et al 2007; van der Meijden et al 2009;Noorduin et al 2010;Blackmond 2011;Coveney et al 2012;Hein et al 2012;Ribó et al 2013;Konstantinova 2013, 2014), and many others. However, most, if not all, theories and experiments related to chiral symmetry breaking during formation of life on Earth considered only a very limited number of substances and reactions, whereas the actual number of possible substances and reactions among them must have been extremely large, as we will soon discuss.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chiral Symmetry Breaking in Peptide Systems During Formation of Life on Earth

Konstantinov

Константинова

2017

Orig Life Evol Biosph

View full text Add to dashboard Cite

Chiral symmetry breaking in complex chemical systems with a large number of amino acids and a large number of similar reactions was considered. It was shown that effective averaging over similar reaction channels may result in very weak effective enantioselectivity of forward reactions, which does not allow most of the known models to result in chiral symmetry breaking during formation of life on Earth. Models with simple and catalytic synthesis of a single amino acid, formation of peptides up to length five, and sedimentation of insoluble pair of substances were considered. It was shown that depending on the model and the values of the parameters, chiral symmetry breaking may occur in up to about 10% out of all possible unique insoluble pair combinations even in the absence of any catalytic synthesis and that minimum total number of amino acids in the pair is 5. If weak enantioselective forward catalytic synthesis of amino acids is present, then the number of possible variants, in which chiral symmetry breaking may occur, increases substantially. It was shown that that the most interesting catalysts have zero or one amino acid of "incorrect" chirality. If the parameters of the model are adjusted in such a way to result in an increase of concentration of longer peptides, then catalysts with two amino acids of incorrect chirality start to appear at peptides of length five. Models of chiral symmetry breaking in the presence of epimerization were considered for peptides up to length three. It was shown that the range of parameters in which chiral symmetry breaking could occur significantly shrinks in comparison to previously considered models with peptides up to length two. An experiment of chiral symmetry breaking was proposed. The experiment consists of a three-step cycle: reversible catalytic synthesis of amino acids, reversible synthesis of peptides, and irreversible sedimentation of insoluble substances.

show abstract

The origin of biological homochirality

Cited by 102 publications

References 27 publications

Principles of protein targeting to the nucleolus

Principles of protein targeting to the nucleolus

Necessary conditions for the emergence of homochirality via autocatalytic self-replication

Chiral Symmetry Breaking in Peptide Systems During Formation of Life on Earth

Contact Info

Product

Resources

About