Abstract
Cytochrome b 5 is an essential electron transfer protein, which is ubiquitously found in living systems and involved in wide variety of biological processes. Tardigrades (also known as water bears), some of which are famous for desiccation resistance, have many proteins unique to them. Here, we report spectroscopic and structural characterization of a cytochrome b 5 like protein from one of the desiccation‐tolerant tardigrades, Ramazzottius varieornatus strain YOKOZUNA‐1 (RvCytb 5). A 1.4 Å resolution crystal structure revealed that RvCytb 5 is a new cytochrome b 5 protein specific to tardigrades.
Highlights
Tardigrades are microscopic multicellular organisms found in almost all environments on Earth from roadside mosses to high mountains and deep sea.[1]
Some terrestrial tardigrades can retain their lives under extremely desiccated conditions through transition into a state called anhydrobiosis, in which metabolic processes are undetectable.[2,3]
Anhydrobiotic tardigrades are known to survive even in space for 10 days.[15]. This extraordinary ability of tardigrades is so famous even in the public that tardigrades appeared in an American famous scifi television series Star Trek and a Japanese magical girl animation series Pretty Cure
Summary
Tardigrades are microscopic multicellular organisms found in almost all environments on Earth from roadside mosses to high mountains and deep sea.[1]. Anhydrobiotic tardigrades are known to survive even in space (low Earth orbit) for 10 days.[15]. This extraordinary ability of tardigrades is so famous even in the public that tardigrades appeared in an American famous scifi television series Star Trek and a Japanese magical girl animation series Pretty Cure. We focus on an electron transfer protein, cytochrome b5 (Cytb5), from tardigrades. The genome of one of the toughest tardigrades, Ramazzottius varieornatus strain YOKOZUNA-1, has several structural genes of Cytb[5] proteins.[22]. Judging from their amino acid sequences, most of them closely resemble well-known Cytb[5] proteins; one cytochrome b5 like (Cytb5-like) protein shows low amino acid sequence similarity to them. We present structural and spectroscopic characterization of this unique Cytb5-like protein from R. varieornatus
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