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Structure of the Replication Terminus--Terminator Protein Complex as Probed by Affinity Cleavage

Structure of the Replication Terminus--Terminator Protein Complex as Probed by Affinity Cleavage

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_38208

Structure of the Replication Terminus--Terminator Protein Complex as Probed by Affinity Cleavage

About this item

Full title

Structure of the Replication Terminus--Terminator Protein Complex as Probed by Affinity Cleavage

Publisher

United States: National Academy of Sciences of the United States of America

Journal title

Proceedings of the National Academy of Sciences - PNAS, 1996-10, Vol.93 (20), p.10647-10652

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences of the United States of America

More information

Scope and Contents

Contents

The replication terminator protein (RTP) of Bacillus subtilis is a homodimer that binds to each replication terminus and impedes replication fork movement in only one orientation with respect to the replication origin. The three-dimensional structure of the TRP--DNA complex needs to be determined to understand how structurally symmetrical dimers of...

Alternative Titles

Full title

Structure of the Replication Terminus--Terminator Protein Complex as Probed by Affinity Cleavage

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_38208

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_38208

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.93.20.10647

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