Extractive institutions in colonial Africa

A common explanation for African current underdevelopment is the extractive character of institutions established during the colonial period. Yet, since colonial extraction is hard to quantify and its exact mechanisms are not well understood, we still do not know precisely how colonial institutions affect economic growth today. In this project, I study this issue by focusing on the peculiar structure of trade and labor policies employed by the French colonizers.

First, I analyze how trade monopsonies and coercive labor institutions reduced African gains from trade during the colonial period. By using new data on prices to agricultural producers and labor institutions in French Africa, I show that (1) the monopsonistic character of colonial trade implied a reduction in prices to producers far below world market prices; (2) coercive labor institutions allowed the colonizers to reduce prices even further; (3) as a consequence, colonial extraction cut African gains from trade by over 60%.

Given the importance of labor institutions, I then focus on their origin by analyzing the colonial governments' incentives to choose between coerced and free labor. I argue that the choice of institutions was affected more by the properties of exported commodities, such as prices and economies of scale, than by the characteristics of colonies, such indigenous population density and ease of settlement for the colonizers.

Finally, I study the long-term effects of colonial trade monopsonies and coercive labor institutions. By combining archival data on prices in the French colonies with maps of crop suitability, I show that the extent to which prices to agricultural producers were reduced with respect to world market prices is strongly negatively correlated with current regional development, as proxied by luminosity data from satellite images. The evidence suggests that colonial extraction affected subsequent growth by reducing development in rural areas in favor of a urban elite. The differential impact in rural and urban areas can be the reason why trade monopsonies and extractive institutions persisted long after independence.

Investigating the Role of the GET3-GET4/GET5 Interaction During Tail-Anchor Protein Targeting

The proper targeting of membrane proteins is essential to the viability of all cells. Tail-anchored (TA) proteins, defined as having a single transmembrane helix at their C-terminus, are post-translationally targeted to the endoplasmic reticulum (ER) membrane by the GET pathway (Guided Entry of TA proteins). In the yeast pathway, the handover of TA substrates is mediated by the heterotetrameric Get4/Get5 (Get4/5) complex, which tethers the co-chaperone Sgt2 to the central targeting factor, the Get3 ATPase. Although binding of Get4/5 to Get3 is critical for efficient TA targeting, the mechanisms by which Get4 regulates Get3 are unknown. To understand the molecular basis of Get4 function, we used a combination of structural biology, biochemistry, and cell biology. Get4/5 binds across the Get3 dimer interface, in an orientation only compatible with a closed Get3, providing insight into the role of nucleotide in complex formation. Additionally, this structure reveals two functionally distinct binding interfaces for anchoring and ATPase regulation, and loss of the regulatory interface leads to strong defects in vitro and in vivo. Additional crystal structures of the Get3-Get4/5 complex give rise to an alternate conformation, which represents an initial binding interaction mediated by electrostatics that facilitates the rate of subsequent inhibited complex formation. This interface is supported by an in-depth kinetic analysis of the Get3-Get4/5 interaction confirming the two-step complex formation. These results allow us to generate a refined model for Get4/5 function in TA targeting.