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Journal of Bacteriology, February 2000, p. 898-904, Vol. 182, No. 4
Microbiology Laboratory, Institute of
Physical and Chemical Research (RIKEN), Wako, Saitama
351-0198,1 and Laboratory of
Molecular Genetics, College of Science, Rikkyo (St. Paul's)
University, Toshima-ku, Tokyo 171-8501,2
Japan
Received 19 August 1999/Accepted 30 November 1999
ShaA (sodium/hydrogen antiporter, previously termed YufT [or
NtrA]), which is responsible for Na+/H+
antiporter activity, is considered to be the major Na+
excretion system in Bacillus subtilis. We found that a
shaA-disrupted mutant of B. subtilis shows
impaired sporulation but normal vegetative growth when the external
Na+ concentration was increased in a low range. In the
shaA mutant,
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Function of a Principal
Na+/H+ Antiporter, ShaA, Is Required for
Initiation of Sporulation in Bacillus subtilis

H-dependent expression of
spo0A (PS) and spoVG at an early
stage of sporulation was sensitive to external NaCl. The level of
H protein was reduced by the addition of NaCl, while the
expression of spo0H, which encodes
H, was
little affected, indicating that posttranscriptional control of
H rather than spo0H transcription is
affected by the addition of NaCl in the shaA mutant. Since
this mutant is considered to have a diminished ability to maintain a
low internal Na+ concentration, an increased level of
internal Na+ may affect posttranscriptional control of
H. Bypassing the phosphorelay by introducing the
sof-1 mutation into this mutant did not restore
spo0A (PS) expression, suggesting that
disruption of shaA affects
H accumulation,
but does not interfere with the phosphorylation and phosphotransfer
reactions of the phosphorelay. These results suggest that ShaA plays a
significant role at an early stage of sporulation and not only during
vegetative growth. Our findings raise the possibility that fine control
of cytoplasmic ion levels, including control of the internal
Na+ concentration, may be important for the progression of
the sporulation process.
*
Corresponding author. Mailing address: Microbiology
Laboratory, Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Phone: 81-48-467-9545. Fax:
81-48-462-4672. E-mail: kosono{at}postman.riken.go.jp.
Present address: National Food Research Institute, Tsukuba, Ibaraki
305-8642, Japan.
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