Most of the early manmade polymers consisted of a repeating monomers.
In proteins - the biological polymers - this is rare. You could have up to
different 20 amino acids in a protein. So when you find a single monomer based protein, you will sit up
and take note. Proteins having long stretches of amino acids like lycine and
glutamate are well documented. But when a protein of more than 300 amino acids
has only the amino acid called serine - well, it becomes serious.
Serine sequences are coded with a lot of degeneracy: there
are six different three letter codes for serine So minor changes in the DNA
code at single nucleotide level does not make much difference to the ultimate
serine sequence. So it is highly conserved.
And usually, if a protein is highly conserved, it must have
some major function. The paper which reports this in a recent issue of the
journal Heredity does not explore the
functions of the protein. But knowing the central role of the amino acid serine
play in the synthesis of nucleotides and also as a precursor to some amino
acids, we should expect that a protein made of serine too has very important
functions in the cell.
The homopolymer of serine was discovered in a soil amoeba
called Dyctyostelium. Dyctyostelium goes through a life cycle consisting of unicellular
and multi-cellular forms and has been
used as a model for understanding social organisation. So we should expect that
such sequences exist in many other organisms soon.
Heredity 112, 215-218 (February 2014) | doi:10.1038/hdy.2013.96