Spatial arrangement of ribosomal proteins: reaction of the Escherichia coli 30S subunit with bis-imidoesters.

Abstract:

:The 30S ribosomal subunit of E. coli was treated with the bifunctional reagent bis-(methyl)suberimidate. Crosslinked ribosomal proteins were identified as bands with increased molecular weight after electrophoresis in polyacrylamide gels containing sodium dodecyl sulphate. The pattern of crosslinked products was altered when unfolded subunits were used. Free ribosomal protein was not crosslinked. Several of the crosslinked products were cleaved by ammonolysis to form the original monomeric protein constituents. The low yields of the reactions necessitated the use of radioactive proteins and auto-radiographic procedures. The crosslinked proteins were tentatively identified by coelectrophoresis of the radioactive ammonolysis products with carrier 30S protein in sodium dodecyl sulphate, and coelectrophoresis at pH 4.5 in buffers containing urea.

authors

Bickle TA,Hershey JW,Traut RR

doi

10.1073/pnas.69.5.1327

subject

Has Abstract

pub_date

1972-05-01 00:00:00

pages

1327-31

issue

5

eissn

0027-8424

issn

1091-6490

journal_volume

69

pub_type

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