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The Dark Matter of Biology - PubMed

  • ️Fri Jan 01 2016

Review

The Dark Matter of Biology

Jennifer L Ross. Biophys J. 2016.

Abstract

The inside of the cell is full of important, yet invisible species of molecules and proteins that interact weakly but couple together to have huge and important effects in many biological processes. Such "dark matter" inside cells remains mostly hidden, because our tools were developed to investigate strongly interacting species and folded proteins. Example dark-matter species include intrinsically disordered proteins, posttranslational states, ion species, and rare, transient, and weak interactions undetectable by biochemical assays. The dark matter of biology is likely to have multiple, vital roles to regulate signaling, rates of reactions, water structure and viscosity, crowding, and other cellular activities. We need to create new tools to image, detect, and understand these dark-matter species if we are to truly understand fundamental physical principles of biology.

Copyright © 2016 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Figures

Figure 1
Figure 1

Calcium waves within Xenopus oocytes imaged using calcium-sensitive dyes. Image used with permission from Science magazine (7).

Figure 2
Figure 2

Percentage of protein sequences with at least one intrinsically disordered region of specified length plotted as a function of the specified length in amino acids. To see this figure in color, go online.

Figure 3
Figure 3

Transient interactions of MAP65 binding to microtubules. (A) Epifluorescence image of microtubules. (B) Individual 100 ms frame of single molecules of GFP-MAP65 binding to microtubules. (C) Merged image of the microtubule (red) and GFP-MAP65 (cyan) to show that some molecules are bound on the microtubules and others are randomly in the background. (D) Kymograph of GFP-MAP65 binding to microtubules (i) or in the background in a region not on microtubules (ii). It is clear that MAP65 interacts more often with the region on the microtubule, but each interaction is brief, one to two frames at 100 ms/frame. (E) Collapsing the movie of GFP-MAP65 by summing the frames confirms the kymograph results that the GFP-MAP65 is binding more frequently to the microtubules than to the background. (F) Merged overlay of microtubules (red) on collapsed movie (cyan) shows an exact correspondence between the GFP-MAP65 binding and the microtubule location. Data are from (58).

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