TY - JOUR
T1 - Two strains of a novel begomovirus encoding Rep proteins with identical β1 strands but different β5 strands are not compatible in replication
AU - Avalos-Calleros, Jesús Aarón
AU - Pastor-Palacios, Guillermo
AU - Bolaños-Martínez, Omayra C.
AU - Mauricio-Castillo, Armando
AU - Gregorio-Jorge, Josefat
AU - Martínez-Marrero, Nadia
AU - Bañuelos-Hernández, Bernardo
AU - Méndez-Lozano, Jesús
AU - Arguello-Astorga, Gerardo Rafael
N1 - Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.
PY - 2021/6
Y1 - 2021/6
N2 - Geminiviruses have genomes composed of single-stranded DNA molecules and encode a rolling-circle replication (RCR) initiation protein (“Rep”), which has multiple functions. Rep binds to specific repeated DNA motifs (“iterons”), which are major determinants of virus-specific replication. The particular amino acid (aa) residues that determine the preference of a geminivirus Rep for specific iterons (i.e., the trans-acting replication “specificity determinants”, or SPDs) are largely unknown, but diverse lines of evidence indicate that most of them are closely associated with the so-called RCR motif I (FLTYP), located in the first 12-19 aa residues of the protein. In this work, we characterized two strains of a novel begomovirus, rhynchosia golden mosaic Sinaloa virus (RhGMSV), that were incompatible in replication in pseudorecombination experiments. Systematic comparisons of the Rep proteins of both RhGMSV strains in the DNA-binding domain allowed the aa residues at positions 71 and 74 to be identified as the residues most likely to be responsible for differences in replication specificity. Residue 71 is part of the β-5 strand structural element, which was predicted in previous studies to contain Rep SPDs. Since the Rep proteins encoded by both RhGMSV strains are identical in their first 24 aa residues, where other studies have mapped potential SPDs, this is the first study lending direct support to the notion that geminivirus Rep proteins contain separate SPDs in their N-terminal domain.
AB - Geminiviruses have genomes composed of single-stranded DNA molecules and encode a rolling-circle replication (RCR) initiation protein (“Rep”), which has multiple functions. Rep binds to specific repeated DNA motifs (“iterons”), which are major determinants of virus-specific replication. The particular amino acid (aa) residues that determine the preference of a geminivirus Rep for specific iterons (i.e., the trans-acting replication “specificity determinants”, or SPDs) are largely unknown, but diverse lines of evidence indicate that most of them are closely associated with the so-called RCR motif I (FLTYP), located in the first 12-19 aa residues of the protein. In this work, we characterized two strains of a novel begomovirus, rhynchosia golden mosaic Sinaloa virus (RhGMSV), that were incompatible in replication in pseudorecombination experiments. Systematic comparisons of the Rep proteins of both RhGMSV strains in the DNA-binding domain allowed the aa residues at positions 71 and 74 to be identified as the residues most likely to be responsible for differences in replication specificity. Residue 71 is part of the β-5 strand structural element, which was predicted in previous studies to contain Rep SPDs. Since the Rep proteins encoded by both RhGMSV strains are identical in their first 24 aa residues, where other studies have mapped potential SPDs, this is the first study lending direct support to the notion that geminivirus Rep proteins contain separate SPDs in their N-terminal domain.
UR - http://www.scopus.com/inward/record.url?scp=85104674117&partnerID=8YFLogxK
U2 - 10.1007/s00705-021-05066-2
DO - 10.1007/s00705-021-05066-2
M3 - Artículo
C2 - 33852083
AN - SCOPUS:85104674117
SN - 0304-8608
VL - 166
SP - 1691
EP - 1709
JO - Archives of Virology
JF - Archives of Virology
IS - 6
ER -