posted on 2012-03-06, 00:00authored byKazumi Sakai, Yasushi Imamoto, Chih-Ying Su, Hisao Tsukamoto, Takahiro Yamashita, Akihisa Terakita, King-Wai Yau, Yoshinori Shichida
Parietopsin is a nonvisual green light-sensitive opsin
closely related to vertebrate visual opsins and was originally identified
in lizard parietal eye photoreceptor cells. To obtain insight into
the functional diversity of opsins, we investigated by UV–visible
absorption spectroscopy the molecular properties of parietopsin and
its mutants exogenously expressed in cultured cells and compared the
properties to those of vertebrate and invertebrate visual opsins.
Our mutational analysis revealed that the counterion in parietopsin
is the glutamic acid (Glu) in the second extracellular loop, corresponding
to Glu181 in bovine rhodopsin. This arrangement is characteristic
of invertebrate rather than vertebrate visual opsins. The photosensitivity
and the molar extinction coefficient of parietopsin were also lower
than those of vertebrate visual opsins, features likewise characteristic
of invertebrate visual opsins. On the other hand, irradiation of parietopsin
yielded meta-I, meta-II, and meta-III intermediates after batho and
lumi intermediates, similar to vertebrate visual opsins. The pH-dependent
equilibrium profile between meta-I and meta-II intermediates was,
however, similar to that between acid and alkaline metarhodopsins
in invertebrate visual opsins. Thus, parietopsin behaves as an “evolutionary
intermediate” between invertebrate and vertebrate visual opsins.