Connecting the Dots: The Effects of Macromolecular Crowding on Cell Physiology

Mourão, Márcio; Hakim, Joe B.; Schnell, Santiago

doi:10.1016/j.bpj.2014.10.051

Cited by 152 publications

(136 citation statements)

References 48 publications

Supporting

Mentioning

132

Contrasting

Order By: Relevance

“…The quantification of how macromolecular crowding affects protein and, in more general, cellular behaviour is of great interest as highlighted by a recent review by Mourao et al Brought to you by | Georgetown University Authenticated Download Date | 8/21/15 11:08 AM 9 / 18 (Mourao et al, 2014). Crowding effects could play a significant role in the formation of large structures in the cytoplasm and nucleoplasm of a living cell, such as cytoskeleton elements or even whole chromosomes (Marenduzzo et al, 2006).…”

Section: Physiological Consequencesmentioning

confidence: 99%

The macromolecular crowding effect – from in vitro into the cell

Gnutt¹,

Ebbinghaus²

2016

Biological Chemistry

101

View full text Add to dashboard Cite

The influence of the cellular milieu, a complex and crowded solvent, is often neglected when biomolecular structure and function are studied in vitro. To mimic the cellular environment, crowding effects are commonly induced in vitro using artificial crowding agents like Ficoll or dextran. However, it is unclear if such effects are also observed in cellulo. Diverging results on protein stability in living cells point out the need for new quantitative methods to investigate the contributions of excluded volume and nonspecific interactions to the cellular crowding effect. We show how new crowding sensitive probes may be utilized to directly investigate crowding effects in living cells. Moreover, we discuss processes where crowding effects could play a crucial role in molecular cell biology.

show abstract

Section: Physiological Consequencesmentioning

confidence: 99%

The macromolecular crowding effect – from in vitro into the cell

Gnutt¹,

Ebbinghaus²

2016

Biological Chemistry

101

View full text Add to dashboard Cite

show abstract

“…In confined or crowded environments, the rates of biochemical reactions can differ markedly from their dilute, well-mixed counterparts (Schnell and Turner, 2004; Zhou et al, 2008; Mourão et al, 2014). Crowding reduces the diffusion coefficient of reactants, slowing diffusion-limited reactions and giving rise to fractal-like reaction kinetics (Kopelman, 1988; Schnell and Turner, 2004; Pitulice et al, 2014).…”

Section: Physiology Of Non-membrane-bound Organelles: Bioreactors mentioning

confidence: 99%

On the origin of non-membrane-bound organelles, and their physiological function

Stroberg

Schnell

2017

Journal of Theoretical Biology

Self Cite

View full text Add to dashboard Cite

The origin of cellular compartmentalization has long been viewed as paralleling the origin of life. Historically, membrane-bound organelles have been presented as the canonical examples of compartmentalization. However, recent interest in cellular compartments that lack encompassing membranes has forced biologists to reexamine the form and function of cellular organization. The intracellular environment is now known to be full of transient macromolecular structures that are essential to cellular function, especially in relation to RNA regulation. Here we discuss key findings regarding the physicochemical principles governing the formation and function of non-membrane bound organelles. Particularly, we focus how the physiological function of non-membrane-bound organelles depends on their molecular structure. We also present a potential mechanism for the formation of non-membrane-bound organelles. We conclude with suggestions for future inquiry into the diversity of roles played by non-membrane bound organelles.

show abstract

“…Protein association is an important center for various cellular processes such as enzyme catalysis, regulation of immune response by cytokines as well as gene regulation, etc [1,2]. Understanding the physical principles governing association mechanisms and rate constants and furthermore, realistically modeling them, are crucial to study the relationship between the cellular structure and function.…”

Section: Introductionmentioning

confidence: 99%

Effect of crowding on protein-protein association in diffusion-limited regime

Jing

Chen

Zhao

2018

J. Phys.: Conf. Ser.

View full text Add to dashboard Cite

Abstract.In the present paper, we establish a theoretical formalism to study the protein-protein association rate in the framework of diffusion-limited theory. To account for the crowding effect due to the presence of polymer, we particularly take into account the deviation of rotational diffusion of proteins from the Stokes-Einstein-Debye relation. Based on fluid mechanics and depletion theory, a new scaling relation for the retardation factor of the rotational diffusion was proposed. Besides, the crowding-induced interaction energy between the proteins has been also properly introduced into the association rate theory. We apply our theory to calculate the association rate constant of proteins β-lactamase and β-lactamase inhibitor protein in poly(ethylene glycol) solutions. Particular attention is paid to the dependence of the association rate constant on the polymer concentration and polymer molecular weight. The deviation from the simple relation based on Stokes-Einstein approximation is well addressed. We find that our theoretical results show good agreements with the experimental data in the whole concentration region, which demonstrates the validity of our theory.

show abstract

Connecting the Dots: The Effects of Macromolecular Crowding on Cell Physiology

Cited by 152 publications

References 48 publications

The macromolecular crowding effect – from in vitro into the cell

The macromolecular crowding effect – from in vitro into the cell

On the origin of non-membrane-bound organelles, and their physiological function

Effect of crowding on protein-protein association in diffusion-limited regime

Contact Info

Product

Resources

About