Biochemical and serological evidence for an RNase E-like activity in halophilic Archaea.

Abstract:

:Endoribonuclease RNase E appears to control the rate-limiting step that mediates the degradation of many mRNA species in bacteria. In this work, an RNase E-like activity in Archaea is described. An endoribonucleolytic activity from the extreme halophile Haloarcula marismortui showed the same RNA substrate specificity as the Escherichia coli RNase E and cross-reacted with a monoclonal antibody raised against E. coli RNase E. The archaeal RNase E activity was partially purified from the extreme halophilic cells and shown, contrary to the E. coli enzyme, to require a high salt concentration for cleavage specificity and stability. These data indicate that a halophilic RNA processing enzyme can specifically recognize and cleave mRNA from E. coli in an extremely salty environment (3 M KCI). Having recently been shown in mammalian cells (A. Wennborg, B. Sohlberg, D. Angerer, G. Klein, and A. von Gabain, Proc. Natl. Acad. Sci. USA 92:7322-7326, 1995), RNase E-like activity has now been identified in all three evolutionary domains: Archaea, Bacteria, and Eukarya. This strongly suggests that mRNA decay mechanisms are highly conserved despite quite different environmental conditions.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Franzetti B,Sohlberg B,Zaccai G,von Gabain A

doi

10.1128/jb.179.4.1180-1185.1997

subject

Has Abstract

pub_date

1997-02-01 00:00:00

pages

1180-5

issue

4

eissn

0021-9193

issn

1098-5530

journal_volume

179

pub_type

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