Minimal and RNA-free RNase P in Aquifex aeolicus
Author(s) -
Astrid I. Nickel,
Nadine B. Wäber,
Markus Gößringer,
Marcus Lechner,
Uwe Linne,
Ursula Toth,
Walter Rossmanith,
Roland K. Hartmann
Publication year - 2017
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1707862114
Subject(s) - aquifex aeolicus , rnase p , rnase ph , rnase mrp , archaea , rna , transfer rna , biology , degradosome , bacteria , enzyme , exosome complex , genetics , non coding rna , rnase h , biochemistry , gene , escherichia coli
Significance RNase P is a tRNA-processing enzyme of unique architectural diversity: either a catalytic RNA plus one or more (up to 10) proteins, or one (or three) unrelated proteins only. We identified yet another enzyme form in the bacteriumAquifex aeolicus , a 23-kDa protein and the smallest known form of RNase P. Apparently, it was acquired by horizontal gene transfer from Archaea. In some other bacteria and many archaea, it is simultaneously present with the presumably more ancient RNA-based enzyme form. Bacteria with both activities may represent the missing link of RNase P evolution, a transition state that had also been once traversed by theAquificaceae , which, however, later lost their RNA-based RNase P.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom