Abstract：
:The primary site of action for the novel antibiotic, bicyclomycin, in Escherichia coli has been identified to be the rho transcription termination factor. The inhibition of rho poly(C)-stimulated hydrolysis of ATP by bicyclomycin has been found to proceed by a non-competitive, reversible pathway with respect to ATP (Ki = 20 microM). Inhibition by dihydrobicyclomycin was similar (Ki = 75 microM). No change in the inhibitory properties of the antibiotic was observed under the assay conditions with the two rho mutants, Cys202Gly and Cys202Ser, indicating that Cys-202 does not affect drug binding to rho. Prolonged incubation (32 degrees C, 12 h) of wild-type rho with bicyclomycin (20 mM) led to protein degradation and a slow, permanent loss of rho ATPase activity after dialysis. Evidence was obtained that trace amounts of proteases present with bicyclomycin were responsible for the observed protein degradation. Treatment of wild-type and mutant rho proteins with purified bicyclomycin (25 mM) led to approximately 80% loss of ATPase activity after dialysis with no apparent loss of protein. However, a reduction of the electrophoretic mobility of the bicyclomycin-treated rho versus wild-type rho was seen. Addition of either ATP or poly(C) to wild-type rho led to partial protection against bicyclomycin inactivation, while inclusion of both ligands provided near complete protection against inactivation. The observed loss of ATPase activity upon prolonged incubation of rho with excess purified bicyclomycin is attributed to the covalent modification of the protein by the antibiotic at multiple sites.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Park HG,Zhang X,Moon HS,Zwiefka A,Cox K,Gaskell SJ,Widger WR,Kohn Hdoi
10.1006/abbi.1995.0066subject
Has Abstractpub_date
1995-11-10 00:00:00pages
447-54issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(85)70066-5journal_volume
323pub_type
杂志文章abstract：:Purification of equilibrative nucleoside transporters has been hampered by the functional instability of the detergent-solubilized proteins. A variety of nonionic detergents were compared with octylglucoside (the most commonly used detergent in this regard) for their abilities to solubilize functionally stable nucleos...
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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pub_type： 杂志文章
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pub_type： 杂志文章
doi：10.1006/abbi.1994.1300
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pub_type： 杂志文章
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
doi：10.1006/abbi.1993.1001
更新日期：1993-01-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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更新日期：1996-09-15 00:00:00
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
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更新日期：2018-04-02 00:00:00
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journal_title：Archives of biochemistry and biophysics
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章,评审
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
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更新日期：1984-02-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1006/abbi.1995.1487
更新日期：1995-10-01 00:00:00
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journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1016/0003-9861(86)90643-0
更新日期：1986-02-01 00:00:00
abstract：:The nucleotide sequence of tyrosine tRNAQ* psi A from bovine liver was determined to be pC-C-U-U-C-m2G-A-U-A-m2G-C-U-C-A-G-D-D-G-G-acp3U-A-G-A -G-C-m22G-m22G -A-G-G-A-C-U-Q*-psi-A-m1G-A-psi m-C-C-U-U-A-G-m7G-D-m5C-G-C-U-G-G-T-psi-C-G-m1A -U-U-C-C-G-G-C-U-C-G-A-A-G-G-A-C-C-AOH. This tyrosine tRNA is 76 nucleotides in l...
journal_title：Archives of biochemistry and biophysics
pub_type： 杂志文章
doi：10.1016/0003-9861(85)90647-2
更新日期：1985-01-01 00:00:00
