Co-evolutional anaylsis of the Na+,K+-ATPase’s β-subunit dimerization

Abstract: Does the active membrane transporter, Na+,K+-ATPase dimerize? If it does, whatis the functional benefit? Does it increase or decrease the turnover rate? Theseare still unanswered questions and current research topics. Previous studies havedemonstrated dimerizations in closely related proteins of the P-type ATPase family.For the Na+, K+-ATPase a first indication of dimerization has been shown viaFluorescence lifetime imaging microscopy (FLIM) or Fluorescence resonance energytransfer - Fluorescence correlation spectroscopy (FRET-FCS) experiments. Theprecise dimer structure, dimerization process, and its ultimate functional effecthowever, remain to be found. This master thesis approaches those questions froma co-evolutionary standpoint. It predicts a possible dimer structure by starting with amultiple sequence alignment, direct coupling analysis, and structural contact filteringalgorithm. This model would strengthen the dimerization model of a decreasedturnover rate due to a competitive behavior of two Na+, K+-ATPases for its energysource ATP.