CPL - Chalmers Publication Library
| Utbildning | Forskning | Styrkeområden | Om Chalmers | In English In English Ej inloggad.

The L2 Loop Peptide of recA Stiffens and restricts Base Motions of Single-stranded DNA Similar to Intact Protein

T. Selmane ; Pernilla Wittung-Stafshede (Institutionen för fysikalisk kemi) ; F. Maraboeuf ; O. Voloshin ; Bengt Nordén (Institutionen för fysikalisk kemi) ; D. Camerini-Otero ; M. Takahashi
FEBS Letters (0014-5793 ). Vol. 446 (1999), 1, p. 30-34.
[Artikel, refereegranskad vetenskaplig]

The L2 loop in the RecA protein is the catalytic center for DNA strand exchange, Here we investigate the DMA binding properties of the L2 loop peptide using optical spectroscopy with polarized light. Both fluorescence intensity and anisotropy of an etheno-modified poly(dA) increase upon peptide binding, indicate that the base motions of single-stranded DNA are restricted in the complex. In agreement with this conclusion, the peptide-poly(dT) complex exhibits a significant linear dichroism signal. The peptide is also found to modify the structure of double-stranded DNA, but does not denature it. It is inferred that strand separation may not be required for the formation of a joint molecule.

Nyckelord: RecA protein, homologous recombination, DNA binding, peptide, DNA base motion

Den här publikationen ingår i följande styrkeområden:

Läs mer om Chalmers styrkeområden  

Denna post skapades 2011-02-18. Senast ändrad 2017-10-03.
CPL Pubid: 136945


Läs direkt!

Länk till annan sajt (kan kräva inloggning)

Institutioner (Chalmers)

Institutionen för fysikalisk kemi (1900-2003)


Nanovetenskap och nanoteknik
Fysikalisk kemi

Chalmers infrastruktur