Comparative study of the N-terminal hydrophilic region in Streptomyces lividans and E. coli FtsY.
Streptomyces lividans FtsY (SlFtsY) was cloned and overexpressed in Escherichia coli. Analysis of the amino acid (aa) sequence showed a concentration of hydrophilic aa's in the N-terminal half region of SlFtsY as observed in that of E. coli FtsY (EcFtsY). However, the length of the hydrophilic region was shorter in SlFtsY than in EcFtsY. Overexpression of SlFtsY in E. coli resulted in growth suppression as in the case of the overexpression of EcFtsY, while growth suppression as a result of the overexpression of the C-terminal half region of SlFtsY was limited. This result suggests that the N-terminal hydrophilic region of SlFtsY, regardless of its short length, would behave like its counterpart region of EcFtsY in E. coli.
Maeda
Isamu
I
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.
Hirose
Nozomi
N
Yamashiro
Hidenori
H
Ichibori
Ayako
A
Ohshima
Shinsuke
S
Fujimoto
Tomonori
T
Kawase
Masaya
M
Yagi
Kiyohito
K
D000596:Amino Acids / Q000032:analysis*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D015870:Gene Expression; D008969:Molecular Sequence Data; D018160:Receptors, Cytoplasmic and Nuclear / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D013302:Streptomyces / Q000737:chemistry / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; C087406:FtsY protein, Bacteria; D018160:Receptors, Cytoplasmic and Nuclear; D011994:Recombinant Proteins