Two segments in bacterial antizyme P22 are essential for binding and enhance degradation of lysine/ornithine decarboxylase in Selenomonas ruminantium.

Abstract:

:In Selenomonas ruminantium, a strictly anaerobic and gram-negative bacterium, the degradation of lysine/ornithine decarboxylase (LDC/ODC) by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain. Amino acid sequence alignment of S. ruminantium P22 with the L10 ribosomal proteins of gram-positive and -negative bacteria showed that P22 has a 5-residue K101NKLD105 segment and an 11-residue G160VIRNAVYVLD170 segment, both of which are lacking in L10 in any other gram-positive and gram-negative bacteria reported. To elucidate whether the two segments are involved in P22 function, a series of mutant genes of P22 were constructed and expressed in Escherichia coli. The proteins were isolated and assayed for their function with respect to S. ruminantium LDC/ODC and mouse ODC. The results indicated that the two segments of P22 are crucial for P22 binding to both enzymes and also accelerated degradation of both decarboxylases.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Yamaguchi Y,Takatsuka Y,Kamio Y

doi

10.1128/JB.01429-07

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

442-6

issue

1

eissn

0021-9193

issn

1098-5530

pii

JB.01429-07

journal_volume

190

pub_type

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