Lysine-2,3-Aminomutase and β-Lysine Acetyltransferase Genes of Methanogenic Archaea Are Salt Induced and Are Essential for the Biosynthesis of N ε -Acetyl-β-Lysine and Growth at High Salinity

Abstract

ABSTRACT The compatible solute N ε -acetyl-β-lysine is unique to methanogenic archaea and is produced under salt stress only. However, the molecular basis for the salt-dependent regulation of N ε -acetyl-β-lysine formation is unknown. Genes potentially encoding lysine-2,3-aminomutase ( ablA ) and β-lysine acetyltransferase ( ablB ), which are assumed to catalyze N ε -acetyl-β-lysine formation from α-lysine, were identified on the chromosomes of the methanogenic archaea Methanosarcina mazei Gö1, Methanosarcina acetivorans , Methanosarcina barkeri , Methanococcus jannaschii , and Methanococcus maripaludis . The order of the two genes was identical in the five organisms, and the deduced proteins were very similar, indicating a high degree of conservation of structure and function. Northern blot analysis revealed that the two genes are organized in an operon (termed the abl operon) in M. mazei Gö1. Expression of the abl operon was strictly salt dependent. The abl operon was deleted in the genetically tractable M. maripaludis . Δ abl mutants of M. maripaludis no longer produced N ε -acetyl-β-lysine and were incapable of growth at high salt concentrations, indicating that the abl operon is essential for N ε -acetyl-β-lysine synthesis. These experiments revealed the first genes involved in the biosynthesis of compatible solutes in methanogens.