McNew, James A.2012-09-062012-09-062012-09-062012-09-062012-052012-09-05May 2012Diaz, Ariel. "The Folding and Binding Partners of the Perlecan SEA Module." (2012) Master’s Thesis, Rice University. <a href="https://hdl.handle.net/1911/64678">https://hdl.handle.net/1911/64678</a>.https://hdl.handle.net/1911/64678Sperm protein, enterokinase and agrin (SEA) modules are small folds within large heavily glycosylated modular proteins. Because decreased expression of SEA-containing proteins such as perlecan (PLN) can lead to diseases such as Schwartz-Jampel syndrome (SJS), characteristics of the PLN SEA module including folding, potential for autocleavage, and protein binding were studied. Sequence analyses, recombinant protein evaluation, and a yeast two-hybrid screen were used to study the PLN SEA module and compare it to the mucin (MUC) 1 SEA module. In silico modeling of the PLN SEA module demonstrated a well conserved α/β sandwich fold. Experiments with expressed proteins showed that unlike MUC1, the PLN SEA module does not autocleave. Two-hybrid screening identified four “high confidence” proteins as potential binding partners which were explored in preliminary experiments. Together, these results demonstrate that PLN SEA module is unique and its properties cannot be generalized with other SEA module proteins such as MUC1.application/pdfengCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.SEA moduleSEA domainPerlecanHSPG2AutocleavageAutoproteolysisMUC1Schwartz-Jampel syndromeThesis2012-09-06123456789/ETD-2012-05-144