Single mutation dramatically changes structure, function of bacteria's transporter proteins

phys.org | 4/25/2019 | Staff
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Swapping a single amino acid in a simple bacterial protein changes its structure and function, revealing the effects of complex gene evolution, finds a new study published in the journal eLife. The study—conducted using E. coli bacteria—can help researchers to better understand the evolution of transporter proteins and their role in drug resistance.

"We were quite surprised by how minor mutations can influence the structure and function of transporter proteins," said Nate Traaseth, associate professor of chemistry at New York University and the study's senior author.

Cells - Membrane - Layer - Interior - Environment

Cells are bound by a thin membrane layer that protects its interior from the outside environment. Within this layer are transporter proteins that control which substances are allowed in and out of the cell. These transporters actively move substances across the cell membrane by loading cargo on one side of the layer, then changing their structure to release it on the other side.

Membrane transporters are typically made up of multiple repeating units. In more complex transporters, the genetic sequence for each of these structural units is fused together into a single gene that codes for the protein.

Pattern - Membrane - Protein - Genes - Advantages

It is thought that the repeated pattern evolved from smaller membrane protein genes that had duplicated and fused together. But are there evolutionary advantages to having more complex transporters being produced from a single, fused gene?

To investigate this, Traaseth and colleagues Maureen Leninger and Ampon (Callie) Sae Her in NYU's Department of Chemistry examined a simple transporter found in E....
(Excerpt) Read more at: phys.org
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