TY  - JOUR
A1  - Rudolf, Mareike
A1  - Tetik, Nalan
A1  - Ramos-León, Félix
A1  - Flinner, Nadine
A1  - Ngo, Giang
A1  - Stevanovic, Mara
A1  - Burnat, Mireia
A1  - Perni, Rafael
A1  - Flores, Enrique
A1  - Schleiff, Enrico
T1  - The Peptidoglycan-binding protein SjcF1 influences septal junction function and channel formation in the filamentous cyanobacterium Anabaena
T2  - mBio
N2  - Filamentous, heterocyst-forming cyanobacteria exchange nutrients and regulators between cells for diazotrophic growth. Two alternative modes of exchange have been discussed involving transport either through the periplasm or through septal junctions linking adjacent cells. Septal junctions and channels in the septal peptidoglycan are likely filled with septal junction complexes. While possible proteinaceous factors involved in septal junction formation, SepJ (FraG), FraC, and FraD, have been identified, little is known about peptidoglycan channel formation and septal junction complex anchoring to the peptidoglycan. We describe a factor, SjcF1, involved in regulation of septal junction channel formation in the heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120. SjcF1 interacts with the peptidoglycan layer through two peptidoglycan-binding domains and is localized throughout the cell periphery but at higher levels in the intercellular septa. A strain with an insertion in sjcF1 was not affected in peptidoglycan synthesis but showed an altered morphology of the septal peptidoglycan channels, which were significantly wider in the mutant than in the wild type. The mutant was impaired in intercellular exchange of a fluorescent probe to a similar extent as a sepJ deletion mutant. SjcF1 additionally bears an SH3 domain for protein-protein interactions. SH3 binding domains were identified in SepJ and FraC, and evidence for interaction of SjcF1 with both SepJ and FraC was obtained. SjcF1 represents a novel protein involved in structuring the peptidoglycan layer, which links peptidoglycan channel formation to septal junction complex function in multicellular cyanobacteria. Nonetheless, based on its subcellular distribution, this might not be the only function of SjcF1.
Y1  - 2015
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/45114
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-451149
SN  - 2150-7511
SN  - 2161-2129
N1  - Copyright © 2015 Rudolf et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited
VL  - 6
IS  - 4, e00376-15
SP  - 1
EP  - 11
PB  - American Society for Microbiology
CY  - Washington, DC
ER  -