Κατεύθυνση Βιοπληροφορική
Library of the School of Science

2021-11-18

2021

Plessas Sotirios

Βασιλική Οικονομίδου, Αναπλ. Καθηγήτρια, Τομέας Βιολογίας Κυττάρου και Βιοφυσικής,
Τμήμα Βιολογίας, Πανεπιστήμιο Αθηνών

Κωνσταντίνος Βοργιάς, Καθηγητής, Τομέας Βιοχημείας, Τμήμα Βιολογίας, Πανεπιστήμιο Αθηνών

Παντελεήμων Μπάγκος, Καθηγητής, Τμήμα Πληροφορικής με Εφαρμογές στη Βιοϊατρική, Πανεπιστήμιο Θεσσαλίας

Υπολογιστικές Μελέτες Μετα-μεταφραστικών Τροποποιήσεων Διαμεμβρανικών Πρωτεΐνών

Greek

Computational Studies of Post – Translation Modifications in Membrane Proteins

Transmembrane proteins are important biomolecules for cellular life, performing many crucial functions, such as enzymatic function, signal transduction, transportation of molecules across the cell membrane, cellular recognition and intracellular joining. Transmembrane proteins are also responsible for other proteins anchoring to specific locations in the cell. Transmembrane proteins are categorized based on the type of polypeptide’s secondary structure which spans the entirety of the lipid bilayer. Two types of integral membrane proteins have been identified, α-helical and β-barrels. For the latter, the strands of polypeptide chain are arranged as a β sheet in the form of a β-barrel (e.g. porin proteins). Proteins perform their biological process and cellular functions through post translational modifications, like phosphorylation and glycosylation. In transmembrane proteins, phosphorylation occurs in intracellular regions while glycosylation takes place in the extracellular matrix. Therefore, the presence of a phosphorylation or glycosylation site in an integral protein provides valuable topological information.
In this study, we identified 54 proteins with experimentally verified post-translational modifications (phosphorylation and glycosylation) which are not located in the transmembrane segments, from the database topPTM. The 54 α-helical transmembrane proteins were trained using pHMMs sequences from PfamA using the HMMER program, in order to identify specific protein domains. These domains are not located in the transmembrane region and contain phosphorylation and glycosylation sites. Through this process we developed a dataset of Pfam domains which are presented in the non-transmembrane segments of α-helical integral membrane proteins, and contain sites of post-translational modifications.
This dataset of unique Pfam domains can be used for future development of improved protein topology prediction algorithms of unknown integral membrane proteins, by providing information for the location of non membrane domains within protein sequence based on the post-translational modifications.

Science

Transmembrane proteins, Post-translation modifications

Yes

1

Yes

125

85

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https://pergamos.lib.uoa.gr/uoa/dl/object/2966065