NMR assignments of the DNA binding domain of Ml4 protein from Mesorhizobium loti.
Ml4 protein from Mesorhizobium loti has a 58% sequence identity with the Ros protein from Agrobacterium tumefaciens that contains a prokaryotic Cys(2)His(2) zinc finger domain. Interestingly, Ml4 is a zinc-lacking protein that does not contain the Cys(2)His(2) motif and is able to bind the Ros DNA target sequence with high affinity. Here we report the (1)H, (15)N and (13)C NMR assignments of the Ml4 protein DNA binding domain (residue 52-151), as an important step toward elucidating at a molecular level how this prokaryotic domain can overcome the metal requirement for proper folding and DNA-binding activity.
Russo
Luigi
L
Dipartimento di Scienze Ambientali, Seconda Università degli Studi di Napoli, via Vivaldi 43, 81100 Caserta, Italy.
Palmieri
Maddalena
M
Baglivo
Ilaria
I
Esposito
Sabrina
S
Isernia
Carla
C
Malgieri
Gaetano
G
Pedone
Paolo V
PV
Fattorusso
Roberto
R
D020561:Alphaproteobacteria / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002247:Carbon Isotopes / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D006859:Hydrogen / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D004268:DNA-Binding Proteins; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D006859:Hydrogen