Disulfide bonds are pivotal for the structure, function, and stability of proteins, and understanding ultraviolet (UV)-induced S-S bond cleavage is highly relevant for elucidating the fundamental mechanisms underlying protein photochemistry. Here, the near-UV photodecomposition mechanisms in gas-phase dimethyl disulfide, a prototype system with a S-S bond, are probed by ultrafast transient X-ray absorption spectroscopy. The evolving electronic structure during and after the dissociation is simultaneously monitored at the sulfur L_1,2,3-edges and the carbon K-edge with 100 fs (FWHM) temporal resolution using the broadband soft X-ray spectrum from a femtosecond high-order harmonics light source. Dissociation products are identified with the help of ADC and RASPT2 electronic-structure calculations. Rapid dissociation into two CH₃S radicals within 120 ± 30 fs is identified as the major relaxation pathway after excitation with 267 nm radiation. Additionally, a 30 ± 10% contribution from asymmetric CH₃S₂ + CH₃ dissociation is indicated by the appearance of CH₃ radicals, which is, however, at least partly the result of multiphoton excitation.