Conserved N-terminal sequences in the flagellins of archaebacteria

Biochemical and Biophysical Research Communications
M L KalmokoffK F Jarrell

Abstract

Methanococcus voltae produces two flagellins of molecular weight 31,000 and 33,000. Amino acid analysis as well as peptide mapping with cyanogen bromide, chymotrypsin and Staphylococcus aureus V-8 protease indicates that the two flagellins are distinct. N-terminal sequencing of the 31,000 Mc. voltae flagellin as well as the 24,000 and 25,000 molecular weight flagellins of Methanospirillum hungatei GP1 shows an extensive homology with the reported N-terminus of the flagellins from Halobacterium halobium, deduced from the nucleotide sequence of the cloned genes. However, the N-termini of all three sequenced methanogen flagellins lack a terminal methionine and start at position 13 from the N-terminus of H. halobium flagellins. This initial 12 amino acid stretch may be a leader peptide which is subsequently cleaved to generate the mature flagellin, which could suggest flagellar assembly in archaebacteria occurs by a mechanism distinct from that in eubacteria. The high degree of conservation of the N-terminus of the flagellins from Mc. voltae, Msp. hungatei and H. halobium suggests an important role for this sequence, and that the archaebacteria share a common mechanism for flagellar biosynthesis.

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Citations

Mar 16, 2001·FEMS Microbiology Reviews·N A ThomasK F Jarrell
Jan 13, 2000·Molecular Microbiology·V Y TarasovO V Fedorov
Dec 1, 1991·Current Opinion in Genetics & Development·W Zillig
Feb 24, 2015·Frontiers in Microbiology·Sonja-Verena Albers, Ken F Jarrell
Mar 10, 2015·Biochemistry. Biokhimii︠a︡·A S SyutkinO V Fedorov
Mar 10, 2020·FEMS Microbiology Reviews·Morgan BeebyDavid R Mitchell
Sep 1, 1996·Journal of Bacteriology·K F JarrellA S Kostyukova
Nov 1, 1991·Journal of Bacteriology·M L Kalmokoff, K F Jarrell

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