1887

Abstract

A temperature-sensitive mutation in designated , encodes a missense mutation at position 142 [His (CAT) to Leu (CTT)] of ribosomal protein L2. The strain carrying the mutation grew more slowly than the wild-type, even at low temperatures, probably due to the formation of defective 70S ribosomes and the accumulation of incomplete 50S subunits (50S* subunits). Gel analysis indicated that amounts of L2 protein and also of L16 protein were reduced in ribosomes prepared from the mutant 90 min after increasing the growth temperature to 45 °C. These results suggest that the assembly of the L16 protein into the 50S subunit requires the native L2 protein. The H142L mutation in the defective L2 protein affected sporulation as well as growth, even at the permissive temperature. A suppressor mutation that restored both growth and sporulation of the mutant at low temperature was identified as a single base deletion located immediately upstream of the gene that resulted in an increase in its transcription. Furthermore, genetic analysis showed that enhanced synthesis of YaaA restores the functionality of L2 (H142L) by facilitating its assembly into 50S subunits.

Funding
This study was supported by the:
  • Ministry of Education, Culture, Sports, Science, and Technology of Japan (Award S1201003)
  • Noda Institute for Scientific Research (NISR)
  • Institute for Fermentation, Osaka
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2014-06-01
2024-04-25
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