TY - JOUR
T1 - Two different types of dehalogenases, LinA and LinB, involved in γ- hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are localized in the periplasmic space without molecular processing
AU - Nagata, Yuji
AU - Futamura, Akiko
AU - Miyauchi, Keisuke
AU - Takagi, Masamichi
PY - 1999/9
Y1 - 1999/9
N2 - γ-Hexachlorocyclohexane (γ-HCH) is one of several highly chlorinated insecticides that cause serious environmental problems. The cellular proteins of a γ-HCH-degrading bacterium, Sphingomonas paucimobilis UT26, were fractionated into periplasmic, cytosolic, and membrane fractions after osmotic shock. Most of two different types of dehalogenase, LinA (γ- hexachlorocyclohexane dehydrochlorinase) and LinB (1,3,4,6-tetrachloro-1,4- cyclohexadiene halidohydrolase), that are involved in the early steps of γ- HCH degradation in UT26 was detected in the periplasmic fraction and had not undertaken molecular processing. Furthermore, immunoelectron microscopy clearly showed that LinA and LinB are periplasmic proteins. LinA and LinB both lack a typical signal sequence for export, so they may be secreted into the periplasmic space via a hitherto unknown mechanism.
AB - γ-Hexachlorocyclohexane (γ-HCH) is one of several highly chlorinated insecticides that cause serious environmental problems. The cellular proteins of a γ-HCH-degrading bacterium, Sphingomonas paucimobilis UT26, were fractionated into periplasmic, cytosolic, and membrane fractions after osmotic shock. Most of two different types of dehalogenase, LinA (γ- hexachlorocyclohexane dehydrochlorinase) and LinB (1,3,4,6-tetrachloro-1,4- cyclohexadiene halidohydrolase), that are involved in the early steps of γ- HCH degradation in UT26 was detected in the periplasmic fraction and had not undertaken molecular processing. Furthermore, immunoelectron microscopy clearly showed that LinA and LinB are periplasmic proteins. LinA and LinB both lack a typical signal sequence for export, so they may be secreted into the periplasmic space via a hitherto unknown mechanism.
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U2 - 10.1128/jb.181.17.5409-5413.1999
DO - 10.1128/jb.181.17.5409-5413.1999
M3 - Article
C2 - 10464214
AN - SCOPUS:0032835982
SN - 0021-9193
VL - 181
SP - 5409
EP - 5413
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 17
ER -